Lecture 4: 8/26. CHAPTER 4 Protein Three Dimensional Structure
|
|
- Ella Ryan
- 5 years ago
- Views:
Transcription
1 Lecture 4: 8/26 CHAPTER 4 Protein Three Dimensional Structure
2 Summary of the Lecture 3 There are 20 amino acids and only the L isomer amino acid exist in proteins Each amino acid consists of a central alpha carbon that is bonded by an amino group, a carboxyl group, a hydrogen atom and distinctive side chain or R group Amino acid can be classified based on the chemical properties of the side chains: 1. Hydrophobic amino acids 2. Polar amino acids 3. Positively charged amino acids 4. Negatively charged amino acids Essential amino acids (9 of them) must be obtained through diet and they are required for healthy growth and development 8/24/2016 2
3 Chapter 4 Outline
4 Polypeptides consist of amino acids linked by a peptide bond. The peptide bond is also called an amide bond. Each amino acid in a protein is called a residue.
5 Peptide bond formation The linking of two amino acids is accompanied by the loss of a molecule of water
6 A polypeptide bond has directionality. The amino terminal end is taken as the beginning of the polypeptide chain. The carboxyl terminal end is the end of the polypeptide chain. The primary structure is always written from the amino terminal to the carboxyl terminal, or left to right.
7 Amino acid sequences have direction Pentapeptide: Tyr Gly Gly Phe Leu (YGGFL) This pentapeptide, Leu enkephalin, is an opioid peptide that modulates the perception of pain.
8 The polypeptide consist of a repeating part called the main chain or backbone and a variable part consisting of the distinctive amino acid side chains. The backbone has hydrogen bonding potential because of the carbonyl groups and hydrogen atoms that are bonded to the nitrogen of the amine group. Most proteins consist of 50 to 2000 amino acids. The mean molecular weight for an amino acid is 110 g mol 1.
9 Components of a polypeptide chain A polypeptide chain consists of a constant backbone (shown in black) and variable side chains (shown in green). Can you identify peptide bound in this polypeptide?
10 In some proteins, the polypeptide chain can be cross linked by disulfide bonds. Disulfide bonds form by the oxidation of two cysteines. The resulting unit of two linked cysteines is called cystine.
11 Cross links between two cysteine amino acids The formation of a disulfide bond between two cysteine residues is an oxidation reaction
12 Amino acid sequence of bovine insulin Genes specify or code amino acid sequences in proteins (hint: central dogma)
13 Quick Quiz What is the amino terminus of a tripeptide Gyl Ala Asp? What is the approximate molecular weight of a protein composed of 300 amino acids? Approximately how many amino acid are required to form a protein with a molecular weight of 10,000?
14 Polypeptide Chains Are Flexible Yet Conformationally Restricted The peptide bond is essentially planar. Six atoms (C α, C, O, N, H, and C α ) lie in a plane. The peptide bond has partial double bond character because of resonance, and thus rotation about the bond is prohibited. Peptide bonds are planar The peptide bond is uncharged.
15 Typical bond lengths within a peptide unit
16 Polypeptide Chains Are Flexible Yet Conformationally Restricted Most peptide bonds are in the trans configuration so as to minimize steric clashes between neighboring R groups.
17 Polypeptide Chains Are Flexible Yet Conformationally Restricted Rotation is permitted about the N C α bond (the phi (Φ )bond) and about C α carbonyl bond (the psi ( ψ) bond.) The rotation about the Φ and ψ bonds, called the torsion angle, determines the path of the polypeptide chain. Not all torsion angles are permitted.
18 Rotation about bonds in a polypeptide
19 A Ramachandran diagram showing the values of Φ and ψ
20 Secondary structure is the three dimensional structure formed by hydrogen bonds between peptide NH and CO groups of amino acids that are near one another in the primary structure. The α helix, β sheets and turns are prominent examples of secondary structure.
21 The Alpha Helix Is a Coiled Structure Stabilized by Intrachain Hydrogen Bonds The α helix is a tightly coiled rod like structure, with the R groups bristling out from the axis of the helix. All of the backbone CO and NH groups form hydrogen bonds except those at the end of the helix. Essentially all α helices found in proteins are right handed.
22 The structure of the a helix
23 The hydrogen bonding scheme for an α helix In the α helix, the CO group of residue i forms a hydrogen bond with the NH group of residue i + 4.
24 Schematic views of a helices (A) A ribbon depiction. (B) A cylindrical depiction.
25 A largely α helical protein Ferritin, an iron storage protein, is built from a bundle of α helices.
26 Beta Sheets Are Stabilized by Hydrogen Bonding Between Polypeptide Strands The β sheet is another common form of secondary structure. Beta sheets are formed by adjacent β strands. In contrast to an α helix, the polypeptide in a β strand is fully extended.
27 The structure of a strand The side chains (green) are alternatively above and below the plane of the strand. The bar shows the distance between two residues.
28 Beta Sheets Are Stabilized by Hydrogen Bonding Between Polypeptide Strands Hydrogen bonds link the strands in a β sheet. The strands of a β sheet may be parallel, antiparallel, or mixed. β sheets may be flat or adopt a twisted conformation.
29 Antiparallel and parallel β sheets Antiparallel β sheets Antiparallel β sheets Parallel β sheets
30 Antiparallel β sheets Adjacent β strands run in opposite directions. Hydrogen bonds (green dashes) between NH and CO groups connect each amino acid to a single amino acid on an adjacent strand, stabilizing the structure.
31 Parallel β sheets Adjacent β strands run in the same direction. Hydrogen bonds connect each amino acid on one strand with two different amino acids on the adjacent strand.
32 The structure of a mixed β sheets
33 A twisted β sheet (A) A schematic model. (B) The schematic view rotated by 90 degrees to illustrate the twist more clearly.
34 A protein rich in β sheet The structure of a fatty acid binding protein
35 Polypeptide Chains Can Change Direction by Making Reverse Turns and Loops The structure of a reverse turn A) The CO group of residue i of the polypeptide chain is hydrogen bonded to the NH group of residue i + 3 to stabilize the turn. B) (B) A part of an antibody molecule has surface loops (shown in red).
36 Fibrous Proteins Provide Structural Support for Cells and Tissues α Keratin, a structural protein found in wool and hair, is composed of two right handed α helices intertwined to form a left handed super helix called a coiled coil. The helices interact with ionic bonds or van der Waals interactions. α Keratin is a member of a superfamily of structural proteins called coiled coil proteins. Other members of the family include some cytoskeleton proteins and muscle proteins.
37 An α helical coiled coil (A) Space filling model. (B) Ribbon diagram. The two helices wind around each other to form a superhelix. Such structures are found in many proteins, including keratin in hair, quills, claws, and horns.
38 Fibrous Proteins Provide Structural Support for Cells and Tissues Collagen is a structural protein that is a component of skin, bone, tendons, cartilage, and teeth. Collagen consists of three intertwined helical polypeptide chains that form a superhelical cable. The helical polypeptide chains of collagen are not α helices. Glycine appears at every third residue and the sequence gly pro pro is common.
39 The amino acid sequence of a part of a collagen chain Every third residue is glycine. Proline and hydroxyproline also are abundant.
40 The conformation of a single strand of a collagen triple helix
41 Fibrous Proteins Provide Structural Support for Cells and Tissues The helices in collagen are not stabilized by hydrogen bonds. Rather, they are stabilized by steric repulsion of the pyrrolidine rings of proline. The three intertwined chains interact with one another with hydrogen bonds. The interior of the superhelical cable is crowded, and only glycine can fit in the interior.
42 The structure of the protein collagen Space filling model of collagen Cross section of a model of collagen
43 Osteogenesis imperfecta, or brittle bone disease, occurs if a mutation results in the substitution of another amino acid in place of glycine.
44 Hydroxyproline, a modified version of proline in which a hydroxyl group replaces a hydrogen, is important for the stabilization of collagen. Vitamin C is required for the formation of hydroxyproline. A lack of vitamin C results in scurvy.
45
46 Tertiary structure refers to the spatial arrangement of amino acids that are far apart in the primary structure and to the pattern of disulfide bond formation.
47 Myoglobin Illustrates the Principles of Tertiary Structure Globular proteins, such as myoglobin, form complicated three dimensional structures. Globular proteins are very compact. There is little or no empty space in the interior of globular proteins. The interior of globular proteins consists mainly of hydrophobic amino acids. The exterior of globular proteins consists of charged and polar amino acids.
48 The three dimensional structure of myoglobin A ribbon diagram A space filling model
49
50 The Tertiary Structure of Many Proteins Can Be Divided into Structural and Functional Units Motifs, or supersecondary structure, are combinations of secondary structure that are found in many proteins. Some proteins have two or more similar or identical compact structures called domains.
51 The helix turn helix motif, a supersecondary structural element Helix turn helix motifs are found in many DNA binding proteins
52 Protein domains The cell surface protein CD4 consists of four similar domains.
53 Many proteins are composed of multiple polypeptide chains called subunits. Such proteins are said to display quaternary structure. Quaternary structure can be as simple as two identical polypeptide chains or as complex as dozens of different polypeptide chains.
54 Quaternary structure The Cro protein of bacteriophage λ is a dimer of identical subunits.
55 The 2 β 2 tetramer of human hemoglobin The ribbon diagram shows that they are composed mainly of helices. The space filling model illustrates the close packing of the atoms and shows that the heme groups (gray) occupy crevices in the protein.
56 Christian Anfinsen placed the enzyme ribonuclease, which degrades RNA, in a solution containing urea and β mercaptoethanol. Urea destroyed all noncovalent bonds, while the β mercaptoethanol destroyed the disulfide bonds. The ribonuclease was denatured. The enzyme displayed no enzymatic activity and existed only as a random coil. When the urea and β mercaptoethanol were slowly removed, the enzyme regained its structure and its activity. Ribonuclease was renatured and attained its normal or native state. These results demonstrated that the information required for a polypeptide chain to fold into a functional protein with a defined threedimensional structure is inherent in the primary structure.
57 Amino acid sequence of bovine ribonuclease The four disulfide bonds are shown in color
58 The role of β mercaptoethanol in reducing disulfide bonds As the disulfides are reduced, the β mercaptoethanol is oxidized and forms dimers
59 The reduction and denaturation of ribonuclease
60 Proteins Fold by the Progressive Stabilization of Intermediates Rather Than by Random Search A monkey randomly poking at a key board could type a sentence from Shakespeare in a few thousand keystrokes if the correct letters are retained, a process called cumulative selection.
61 Proteins Fold by the Progressive Stabilization of Intermediates Rather Than by Random Search Protein folding is often represented as a folding funnel. The protein has maximum entropy and minimal structure at the top of the funnel. The folded protein exists at the bottom of the funnel. Folding funnel: The folding funnel depicts the thermodynamics of protein folding
62 Some Proteins Are Inherently Unstructured and Can Exist in Multiple Conformations Intrinsically unstructured proteins (IUP) do not have a defined structure under physiological conditions until they interact with other molecules. Metamorphic proteins exist in an ensemble of structures of approximately equal energies that are in equilibrium. Lymphotactin exists in two conformations, which are in equilibrium
63 Amyloidoses are diseases that result from the formation of protein aggregates, called amyloid fibrils or plaques. Alzheimer disease is an example of an amyloidosis. PET scan of the brain of a normal person PET scan of the brain of Alzheimer patient Colored positron emission tomography (PET) scans of the brain of a normal person (left) and that of a patient who has Alzheimer disease (right). Color coding: high brain activity (red and yellow); low activity (blue and black). The Alzheimer patient s scan shows severe deterioration of brain activity.
64 Some infectious neurological diseases are caused by infectious proteins called prions. Prions exist in two states, one α helix rich (PrP) and the other β sheet rich (PrP SC ). PrP SC forms aggregates that disrupt cell function. The protein only model for prion disease transmission A nucleus consisting of proteins in an abnormal conformation grows by the addition of proteins from the normal pool.
65 Summary of the Lecture 4 Primary structure: Amino acids (aa) are linked by peptide bond or amide bond to form polypeptide chains Peptide bonds form between the carboxyl group (the H bond acceptor) of one aa and the amino group (the H bond donor) of the next aa. Significance: (a) Peptide bond is resistant to hydrolysis, and thus proteins are remarkably stable. (b) Each polypeptide bond has both a H bond donor (the NH group) and a H bond acceptor (the CO group) Proteins are sequence of amino acids and the sequences are written from the amino (NH) to the carboxyl (CO) terminus Secondary Structure: Polypeptide can fold into regular structures The a helix and b strand are the two major elements of the secondary structure. In the helix, polypeptide chain twists into tightly packed rod. Within the a helix, the CO group of each aa is H bonded to the NH group of the aa In the b strand, the polypeptide chain is nearly fully extended. Two or more b strand connected by NH to CO hydrogen bond come together to form b sheets. The strand of b sheets can be parallel, antiparallel, or mixed
66 Summary of the Lecture 4 (Continued) Tertiary structure: Water soluble proteins fold into compact structure. Amino acids with hydrophobic side chains are located in interior of the structure. Amino acids with hydrophilic side chains are largely located in surface of the structure and interact with aqueous environment The driving force of the formation of tertiary structure of water soluble proteins is the hydrophobic interaction between the interior residues Quaternary Structure: two or more polypeptide chains can assemble into a single protein. Each individual polypeptide is called a subunit. Subunit held together by noncovalent bonds The amino acid sequence of a protein determines its 3 D structure. The sequences of the bases in a DNA molecules determine the aa sequence of a protein Proper folding of a protein is important its intended function. Improper proper protein folding can cause diseases such Alzheimer disease
The three important structural features of proteins:
The three important structural features of proteins: a. Primary (1 o ) The amino acid sequence (coded by genes) b. Secondary (2 o ) The interaction of amino acids that are close together or far apart in
More informationProtein Secondary Structure
Protein Secondary Structure Reading: Berg, Tymoczko & Stryer, 6th ed., Chapter 2, pp. 37-45 Problems in textbook: chapter 2, pp. 63-64, #1,5,9 Directory of Jmol structures of proteins: http://www.biochem.arizona.edu/classes/bioc462/462a/jmol/routines/routines.html
More informationProteins consist of joined amino acids They are joined by a Also called an Amide Bond
Lecture Two: Peptide Bond & Protein Structure [Chapter 2 Berg, Tymoczko & Stryer] (Figures in Red are for the 7th Edition) (Figures in Blue are for the 8th Edition) Proteins consist of joined amino acids
More informationChem Lecture 2 Protein Structure
Chem 452 - Lecture 2 Protein Structure 110923 Proteins are the workhorses of a living cell and involve themselves in nearly all of the activities that take place in a cell. Their wide range of structures
More informationStructure of proteins
Structure of proteins Presented by Dr. Mohammad Saadeh The requirements for the Pharmaceutical Biochemistry I Philadelphia University Faculty of pharmacy Structure of proteins The 20 a.a commonly found
More informationProtein structure. Dr. Mamoun Ahram Summer semester,
Protein structure Dr. Mamoun Ahram Summer semester, 2017-2018 Overview of proteins Proteins have different structures and some have repeating inner structures, other do not. A protein may have gazillion
More informationProteins and their structure
Proteins and their structure Proteins are the most abundant biological macromolecules, occurring in all cells and all parts of cells. Proteins also occur in great variety; thousands of different kinds,
More informationLevels of Protein Structure:
Levels of Protein Structure: PRIMARY STRUCTURE (1 ) - Defined, non-random sequence of amino acids along the peptide backbone o Described in two ways: Amino acid composition Amino acid sequence M-L-D-G-C-G
More informationNafith Abu Tarboush DDS, MSc, PhD
Nafith Abu Tarboush DDS, MSc, PhD natarboush@ju.edu.jo www.facebook.com/natarboush Protein conformation Many conformations are possible for proteins due to flexibility of amino acids linked by peptide
More informationProtein Structure and Function
Protein Structure and Function Protein Structure Classification of Proteins Based on Components Simple proteins - Proteins containing only polypeptides Conjugated proteins - Proteins containing nonpolypeptide
More informationProteins are linear polymers built of monomer units called amino acids. Proteins contain a wide range of functional groups.
Chapter 2: Protein Structure and Function Proteins arevery versatile with regards to functions for the cell Uses? Proteins are linear polymers built of monomer units called amino acids. One dimensional
More informationChemistry 20 Chapter 14 Proteins
Chapter 14 Proteins Proteins: all proteins in humans are polymers made up from 20 different amino acids. Proteins provide structure in membranes, build cartilage, muscles, hair, nails, and connective tissue
More informationSheet #5 Dr. Mamoun Ahram 8/7/2014
P a g e 1 Protein Structure Quick revision - Levels of protein structure: primary, secondary, tertiary & quaternary. - Primary structure is the sequence of amino acids residues. It determines the other
More information!"#$%&' (#%) /&'(2+"( /&3&4,, ! " #$% - &'()!% *-sheet -(!-Helix - &'(&') +,(-. - &'()&+) /&%.(0&+(! - &'(1&2%( Basic amino acids
Basic amino acids pk ~ 10.5 pk ~ 12.5 pk ~ 6.0 Polar 25!"#$%&' (#%)! " #$% - &'()!% *-sheet -(!-Helix - &'(&') +,(-. - &'()&+) /&%.(0&+(! - &'(1&2%( /&'(2+"( /&3&4,, :++55 ('&.! 6($.(" 40 > 3&4,, ('&.!
More informationBIO 311C Spring Lecture 15 Friday 26 Feb. 1
BIO 311C Spring 2010 Lecture 15 Friday 26 Feb. 1 Illustration of a Polypeptide amino acids peptide bonds Review Polypeptide (chain) See textbook, Fig 5.21, p. 82 for a more clear illustration Folding and
More information4. THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS
4. THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS 4.1 Proteins Structures and Function Levels of Structure in Proteins Native conformation - Biological activity - Random structure: no obvious regular repeating
More informationBCH Graduate Survey of Biochemistry
BCH 5045 Graduate Survey of Biochemistry Instructor: Charles Guy Producer: Ron Thomas Director: Glen Graham Lecture 10 Slide sets available at: http://hort.ifas.ufl.edu/teach/guyweb/bch5045/index.html
More informationAmino Acids and Proteins Hamad Ali Yaseen, PhD MLS Department, FAHS, HSC, KU Biochemistry 210 Chapter 22
Amino Acids and Proteins Hamad Ali Yaseen, PhD MLS Department, FAHS, HSC, KU Hamad.ali@hsc.edu.kw Biochemistry 210 Chapter 22 Importance of Proteins Main catalysts in biochemistry: enzymes (involved in
More informationSRTUCTURE OF PROTEINS DR. A. TARAB DEPT. OF BIOCHEMISTRY HKMU
SRTUCTURE OF PROTEINS DR. A. TARAB DEPT. OF BIOCHEMISTRY HKMU I. OVERVIEW The twenty amino acids commonly found in proteins are joined together by peptide bonds The linear sequence of the linked amino
More informationThe Structure and Function of Large Biological Molecules Part 4: Proteins Chapter 5
Key Concepts: The Structure and Function of Large Biological Molecules Part 4: Proteins Chapter 5 Proteins include a diversity of structures, resulting in a wide range of functions Proteins Enzymatic s
More informationMultiple-Choice Questions Answer ALL 20 multiple-choice questions on the Scantron Card in PENCIL
Multiple-Choice Questions Answer ALL 20 multiple-choice questions on the Scantron Card in PENCIL For Questions 1-10 choose ONE INCORRECT answer. 1. Which ONE of the following statements concerning the
More informationAmino Acids. Review I: Protein Structure. Amino Acids: Structures. Amino Acids (contd.) Rajan Munshi
Review I: Protein Structure Rajan Munshi BBSI @ Pitt 2005 Department of Computational Biology University of Pittsburgh School of Medicine May 24, 2005 Amino Acids Building blocks of proteins 20 amino acids
More informationOrganic Molecules: Proteins
Organic Molecules: Proteins Proteins Most structurally & functionally diverse group Function: involved in almost everything enzymes (pepsin, DNA polymerase) structure (keratin, collagen) carriers & transport
More informationQ1: Circle the best correct answer: (15 marks)
Q1: Circle the best correct answer: (15 marks) 1. Which one of the following incorrectly pairs an amino acid with a valid chemical characteristic a. Glycine, is chiral b. Tyrosine and tryptophan; at neutral
More informationLecture 15. Membrane Proteins I
Lecture 15 Membrane Proteins I Introduction What are membrane proteins and where do they exist? Proteins consist of three main classes which are classified as globular, fibrous and membrane proteins. A
More informationPeptides. The two amino acids are joined through a dehydration reaction.
Peptides Peptides The two amino acids are joined through a dehydration reaction. Peptides The Peptide Bond The peptide bond is usually drawn as a single bond, but actually has considerable double bond
More informationCopyright Mark Brandt, Ph.D. 46
Examples of tein Structures tein types teins fall into three general classes, based on their overall three-dimensional structure and on their functional role: fibrous, membrane, and globular. Fibrous proteins
More informationCopyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
Concept 5.4: Proteins have many structures, resulting in a wide range of functions Proteins account for more than 50% of the dry mass of most cells Protein functions include structural support, storage,
More informationProtein Classification based upon Biological functions
PROTEINS (a) The light produced by fireflies is the result of a reaction involving the protein luciferin and ATP, catalyzed by the enzyme luciferase. (b) Erythrocytes contain large amounts of the oxygen-transporting
More informationCh5: Macromolecules. Proteins
Ch5: Macromolecules Proteins Essential Knowledge 4.A.1 The subcomponents of biological molecules and their sequence determine the properties of that molecule A. Structure and function of polymers are derived
More informationIonization of amino acids
Amino Acids 20 common amino acids there are others found naturally but much less frequently Common structure for amino acid COOH, -NH 2, H and R functional groups all attached to the a carbon Ionization
More informationBioinformatics for molecular biology
Bioinformatics for molecular biology Structural bioinformatics tools, predictors, and 3D modeling Structural Biology Review Dr Research Scientist Department of Microbiology, Oslo University Hospital -
More informationRaghad Abu Jebbeh. Amani Nofal. Mamoon Ahram
... 14 Raghad Abu Jebbeh Amani Nofal Mamoon Ahram This sheet includes part of lec.13 + lec.14. Amino acid peptide protein Terminology: 1- Residue: a subunit that is a part of a large molecule. 2- Dipeptide:
More informationAmino Acids and Proteins (2) Professor Dr. Raid M. H. Al-Salih
Amino Acids and Proteins (2) Professor Dr. Raid M. H. Al-Salih 1 Some important biologically active peptides 2 Proteins The word protein is derived from Greek word, proteios which means primary. As the
More informationThe Basics: A general review of molecular biology:
The Basics: A general review of molecular biology: DNA Transcription RNA Translation Proteins DNA (deoxy-ribonucleic acid) is the genetic material It is an informational super polymer -think of it as the
More informationCS612 - Algorithms in Bioinformatics
Spring 2016 Protein Structure February 7, 2016 Introduction to Protein Structure A protein is a linear chain of organic molecular building blocks called amino acids. Introduction to Protein Structure Amine
More information! Proteins are involved functionally in almost everything: " Receptor Proteins - Respond to external stimuli. " Storage Proteins - Storing amino acids
Proteins Most structurally & functionally diverse group! Proteins are involved functionally in almost everything: Proteins Multi-purpose molecules 2007-2008 Enzymatic proteins - Speed up chemical reactions!
More informationMolecular Biology. general transfer: occurs normally in cells. special transfer: occurs only in the laboratory in specific conditions.
Chapter 9: Proteins Molecular Biology replication general transfer: occurs normally in cells transcription special transfer: occurs only in the laboratory in specific conditions translation unknown transfer:
More informationBiology 5A Fall 2010 Macromolecules Chapter 5
Learning Outcomes: Macromolecules List and describe the four major classes of molecules Describe the formation of a glycosidic linkage and distinguish between monosaccharides, disaccharides, and polysaccharides
More informationProteins: Structure and Function 2/8/2017 1
Proteins: Structure and Function 2/8/2017 1 outline Protein functions hemistry of amino acids Protein Structure; Primary structure Secondary structure Tertiary structure Quaternary structure 2/8/2017 2
More informationThe Structure and Func.on of Macromolecules Proteins GRU1L6
The Structure and Func.on of Macromolecules Proteins GRU1L6 Proteins Proteins Most structurally & functionally diverse group Function: involved in almost everything enzymes (pepsin, DNA polymerase) structure
More informationNafith Abu Tarboush DDS, MSc, PhD
Nafith Abu Tarboush DDS, MSc, PhD natarboush@ju.edu.jo www.facebook.com/natarboush Types of proteins Proteins can be divided into two groups according to structure: Fibrous (fiber-like with a uniform secondary-structure
More informationObjective: You will be able to explain how the subcomponents of
Objective: You will be able to explain how the subcomponents of nucleic acids determine the properties of that polymer. Do Now: Read the first two paragraphs from enduring understanding 4.A Essential knowledge:
More informationThis exam consists of two parts. Part I is multiple choice. Each of these 25 questions is worth 2 points.
MBB 407/511 Molecular Biology and Biochemistry First Examination - October 1, 2002 Name Social Security Number This exam consists of two parts. Part I is multiple choice. Each of these 25 questions is
More informationH C. C α. Proteins perform a vast array of biological function including: Side chain
Topics The topics: basic concepts of molecular biology elements on Python overview of the field biological databases and database searching sequence alignments phylogenetic trees microarray data analysis
More informationProteins. (b) Protein Structure and Conformational Change
Proteins (b) Protein Structure and Conformational Change Protein Structure and Conformational Change Proteins contain the elements carbon (C), hydrogen (H), oxygen (O2) and nitrogen (N2) Some may also
More informationBiochemistry by Mary K. Campbell & Shawn O. Farrell
4 Biochemistry by Mary K. Campbell & Shawn O. Farrell 4-1 4 The ThreeDimensional Structure of Proteins 4-2 4 Learning Objectives 1. How does the Structure of Proteins Determine Their Function? 2. What
More informationAP Bio. Protiens Chapter 5 1
Concept.4: Proteins have many structures, resulting in a wide range of functions Proteins account for more than 0% of the dry mass of most cells Protein functions include structural support, storage, transport,
More informationPolypeptides and Proteins
Polypeptides and Proteins These molecules are composed, at least in part, of chains of amino acids. Each amino acid is joined to the next one through an amide or peptide bond from the carbonyl carbon of
More informationChapter 20 and GHW#10 Questions. Proteins
Chapter 20 and GHW#10 Questions Proteins Proteins Naturally occurring bioorganic polyamide polymers containing a sequence of various combinations of 20 amino acids. Amino acids contain the elements carbon,
More informationSheet #8 Dr. Nafeth Abu-Tarboush 13/07/2014
Done by 1 Ali Khresat Structure-function relationship of proteins we have talked about proteins, the structure of proteins and features of proteins now we will talk about how this structure is related
More informationIntroduction to proteins and protein structure
Introduction to proteins and protein structure The questions and answers below constitute an introduction to the fundamental principles of protein structure. They are all available at [link]. What are
More informationLecture 5. Secondary Structure of Proteins. "-Pleated Sheet. !-Helix. Examples of Protein Structures
econdary tructure of Proteins Lecture 5 Proteins- tructure and Properties Chapter 21 ections 7-11! There are two main aspects of 2 o structure!the type of fold or bend in the protein chain!the types of
More informationBiological systems interact, and these systems and their interactions possess complex properties. STOP at enduring understanding 4A
Biological systems interact, and these systems and their interactions possess complex properties. STOP at enduring understanding 4A Homework Watch the Bozeman video called, Biological Molecules Objective:
More informationBIOB111 - Tutorial activity for Session 14
BIOB111 - Tutorial activity for Session 14 General topics for week 7 Session 14 Amino acids and proteins Students review the concepts learnt and answer the selected questions from the textbook. General
More informationBiology 2E- Zimmer Protein structure- amino acid kit
Biology 2E- Zimmer Protein structure- amino acid kit Name: This activity will use a physical model to investigate protein shape and develop key concepts that govern how proteins fold into their final three-dimensional
More informationIntroduction to Proteomics Dr. Sanjeeva Srivastava Department of Biosciences and Bioengineering Indian Institute of Technology - Bombay
Introduction to Proteomics Dr. Sanjeeva Srivastava Department of Biosciences and Bioengineering Indian Institute of Technology - Bombay Lecture 01 Introduction to Amino Acids Welcome to the proteomic course.
More informationChemistry B11 Chapters 16 Proteins and Enzymes
Chapters 16 Proteins and Enzymes Proteins: all proteins in humans are polymers made up from 20 different amino acids. Proteins provide structure in membranes, build cartilage, muscles, hair, nails, and
More informationThe Structure and Function of Macromolecules
The Structure and Function of Macromolecules Macromolecules are polymers Polymer long molecule consisting of many similar building blocks. Monomer the small building block molecules. Carbohydrates, proteins
More informationBiomolecules: amino acids
Biomolecules: amino acids Amino acids Amino acids are the building blocks of proteins They are also part of hormones, neurotransmitters and metabolic intermediates There are 20 different amino acids in
More informationSecondary Structure. by hydrogen bonds
Secondary Structure In the previous protein folding activity, you created a hypothetical 15-amino acid protein and learned that basic principles of chemistry determine how each protein spontaneously folds
More informationNafith Abu Tarboush DDS, MSc, PhD
Nafith Abu Tarboush DDS, MSc, PhD natarboush@ju.edu.jo www.facebook.com/natarboush http://eacademic.ju.edu.jo/n.abutarboush/material/forms/allitems.aspx Biological Functions of Proteins Enzymes--catalysts
More informationGlobular proteins Proteins globular fibrous
Globular proteins Globular proteins Proteins are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form in a biologically functional way. Globular
More informationBiochemistry 15 Doctor /7/2012
Heme The Heme is a chemical structure that diffracts by light to give a red color. This chemical structure is introduced to more than one protein. So, a protein containing this heme will appear red in
More informationPaper No. 01. Paper Title: Food Chemistry. Module-16: Protein Structure & Denaturation
Paper No. 01 Paper Title: Food Chemistry Module-16: Protein Structure & Denaturation The order of amino acids in a protein molecule is genetically determined. This primary sequence of amino acids must
More informationMacromolecules Structure and Function
Macromolecules Structure and Function Within cells, small organic molecules (monomers) are joined together to form larger molecules (polymers). Macromolecules are large molecules composed of thousands
More informationChapter 6 - Proteins: Three Dimensional Structure
Chapter 6 - Proteins: Three Dimensional Structure Introduction: The first x-ray structure for a protein was that for myoglobin in 1958 and indicated an apparent lack of regularity in the structure. Although
More informationSecondary Structure North 72nd Street, Wauwatosa, WI Phone: (414) Fax: (414) dmoleculardesigns.com
Secondary Structure In the previous protein folding activity, you created a generic or hypothetical 15-amino acid protein and learned that basic principles of chemistry determine how each protein spontaneously
More informationStructural Bioinformatics (C3210) Protein Structure
Structural Bioinformatics (C3210) Protein Structure Great Diversity of Protein Biological Functions The primary responsibility of proteins is to execute the tasks directed by genomic information. The proteins
More informationOPTION GROUP: BIOLOGICAL MOLECULES 3 PROTEINS WORKBOOK. Tyrone R.L. John, Chartered Biologist
NAME: OPTION GROUP: BIOLOGICAL MOLECULES 3 PROTEINS WORKBOOK Tyrone R.L. John, Chartered Biologist 1 Tyrone R.L. John, Chartered Biologist 2 Instructions REVISION CHECKLIST AND ASSESSMENT OBJECTIVES Regular
More informationpaper and beads don t fall off. Then, place the beads in the following order on the pipe cleaner:
Beady Pipe Cleaner Proteins Background: Proteins are the molecules that carry out most of the cell s dayto-day functions. While the DNA in the nucleus is "the boss" and controls the activities of the cell,
More informationChapter 5 Structure and Function Of Large Biomolecules
Formation of Macromolecules Monomers Polymers Macromolecules Smaller larger Chapter 5 Structure and Function Of Large Biomolecules monomer: single unit dimer: two monomers polymer: three or more monomers
More informationReview II: The Molecules of Life
Review II: The Molecules of Life Judy Wieber BBSI @ Pitt 2007 Department of Computational Biology University of Pittsburgh School of Medicine May 24, 2007 Outline Introduction Proteins Carbohydrates Lipids
More informationMethionine (Met or M)
Fig. 5-17 Nonpolar Fig. 5-17a Nonpolar Glycine (Gly or G) Alanine (Ala or A) Valine (Val or V) Leucine (Leu or L) Isoleucine (Ile or I) Methionine (Met or M) Phenylalanine (Phe or F) Polar Trypotphan (Trp
More informationUnderstand how protein is formed by amino acids
Identify between fibrous and globular proteins Understand how protein is formed by amino acids Describe the structure of proteins using specific examples Functions of proteins Fibrous proteins Globular
More informationAmino acids & Protein Structure Chemwiki: Chapter , with most emphasis on 16.3, 16.4 and 16.6
Amino acids & Protein Structure Chemwiki: Chapter 16. 16.1, 16.3-16.9 with most emphasis on 16.3, 16.4 and 16.6 1 1. Most jobs (except information storage) in cells are performed by proteins. 2. Proteins
More informationa) The statement is true for X = 400, but false for X = 300; b) The statement is true for X = 300, but false for X = 200;
1. Consider the following statement. To produce one molecule of each possible kind of polypeptide chain, X amino acids in length, would require more atoms than exist in the universe. Given the size of
More informationChemical Nature of the Amino Acids. Table of a-amino Acids Found in Proteins
Chemical Nature of the Amino Acids All peptides and polypeptides are polymers of alpha-amino acids. There are 20 a- amino acids that are relevant to the make-up of mammalian proteins (see below). Several
More informationBIRKBECK COLLEGE (University of London)
BIRKBECK COLLEGE (University of London) SCHOOL OF BIOLOGICAL SCIENCES M.Sc. EXAMINATION FOR INTERNAL STUDENTS ON: Postgraduate Certificate in Principles of Protein Structure MSc Structural Molecular Biology
More informationProteins. Amino acids, structure and function. The Nobel Prize in Chemistry 2012 Robert J. Lefkowitz Brian K. Kobilka
Proteins Amino acids, structure and function The Nobel Prize in Chemistry 2012 Robert J. Lefkowitz Brian K. Kobilka O O HO N N HN OH Ser65-Tyr66-Gly67 The Nobel prize in chemistry 2008 Osamu Shimomura,
More informationChapter 21 Lecture Outline
Chapter 21 Lecture Outline Amino Acids, Proteins, and Enzymes! Introduction! Proteins are biomolecules that contain many amide bonds, formed by joining amino acids. Prepared by Andrea D. Leonard University
More informationJudy Wieber. Department of Computational Biology. May 27, 2008
Review II: The Molecules of Life Judy Wieber BBSI @ Pitt 2008 Department of Computational Biology University it of Pittsburgh School of Medicine i May 27, 2008 Outline Introduction Proteins Carbohydrates
More information1. Structure, classification, functions, properties of proteins
1. Structure, classification, functions, properties of proteins Proteins are the major components of living organisms and perform a wide range of essential functions in cells. Proteins regulate metabolic
More informationPHAR3316 Pharmacy biochemistry Exam #2 Fall 2010 KEY
1. How many protons is(are) lost when the amino acid Asparagine is titrated from its fully protonated state to a fully deprotonated state? A. 0 B. 1 * C. 2 D. 3 E. none Correct Answer: C (this question
More informationMacromolecules of Life -3 Amino Acids & Proteins
Macromolecules of Life -3 Amino Acids & Proteins Shu-Ping Lin, Ph.D. Institute of Biomedical Engineering E-mail: splin@dragon.nchu.edu.tw Website: http://web.nchu.edu.tw/pweb/users/splin/ Amino Acids Proteins
More informationBIOCHEMISTRY Amino Acids and Proteins
BIOCHEMISTRY Amino Acids and Proteins BIOB111 CHEMISTRY & BIOCHEMISTRY Session 14 Session Plan Characteristics of Proteins Amino Acids: Building Blocks for Proteins Essential Amino Acids Properties of
More informationAMINO ACIDS AND PROTEINS. HLeeYu Jsuico Junsay Department of Chemistry School of Science and Engineering Ateneo de Manila University
AMINO ACIDS AND PROTEINS HLeeYu Jsuico Junsay Department of Chemistry School of Science and Engineering Ateneo de Manila University 1 Proteins serves as the cell s machinery as well as an organism s other
More informationProteins. Proteins. Proteins. Proteins. Effect of different R groups: Nonpolar amino acids. Amino acids H C OH H R. Multipurpose molecules.
Multipurpose molecules 2008-2009 Most structurally & functionally diverse group Function: involved in almost everything enzymes (pepsin, DNA polymerase) structure (keratin, collagen) carriers & transport
More informationTHE UNIVERSITY OF MANITOBA. DATE: Oct. 22, 2002 Midterm EXAMINATION. PAPER NO.: PAGE NO.: 1of 6 DEPARTMENT & COURSE NO.: 2.277/60.
PAPER NO.: PAGE NO.: 1of 6 GENERAL INSTRUCTIONS You must mark the answer sheet with pencil (not pen). Put your name and enter your student number on the answer sheet. The examination consists of multiple
More informationLecture Series 2 Macromolecules: Their Structure and Function
Lecture Series 2 Macromolecules: Their Structure and Function Reading Assignments Read Chapter 4 (Protein structure & Function) Biological Substances found in Living Tissues The big four in terms of macromolecules
More informationLecture 10 More about proteins
Lecture 10 More about proteins Today we're going to extend our discussion of protein structure. This may seem far-removed from gene cloning, but it is the path to understanding the genes that we are cloning.
More informationLecture Series 2 Macromolecules: Their Structure and Function
Lecture Series 2 Macromolecules: Their Structure and Function Reading Assignments Read Chapter 4 (Protein structure & Function) Biological Substances found in Living Tissues The big four in terms of macromolecules
More informationOPTION GROUP: BIOLOGICAL MOLECULES 3 PROTEINS WORKBOOK. Tyrone R.L. John, Chartered Biologist
NAME: OPTION GROUP: BIOLOGICAL MOLECULES 3 PROTEINS WORKBOOK Tyrone R.L. John, Chartered Biologist 1 Tyrone R.L. John, Chartered Biologist 2 Instructions REVISION CHECKLIST AND ASSESSMENT OBJECTIVES Regular
More informationPROTEINS. Amino acids are the building blocks of proteins. Acid L-form * * Lecture 6 Macromolecules #2 O = N -C -C-O.
Proteins: Linear polymers of amino acids workhorses of the cell tools, machines & scaffolds Lecture 6 Macromolecules #2 PRTEINS 1 Enzymes catalysts that mediate reactions, increase reaction rate Structural
More informationShort polymer. Dehydration removes a water molecule, forming a new bond. Longer polymer (a) Dehydration reaction in the synthesis of a polymer
HO 1 2 3 H HO H Short polymer Dehydration removes a water molecule, forming a new bond Unlinked monomer H 2 O HO 1 2 3 4 H Longer polymer (a) Dehydration reaction in the synthesis of a polymer HO 1 2 3
More informationWhat are the molecules of life?
Molecules of Life What are the molecules of life? Organic Compounds Complex Carbohydrates Lipids Proteins Nucleic Acids Organic Compounds Carbon- hydrogen based molecules From Structure to Function Ø Carbon
More informationChapter 5: Outline. Protein Function. Proteins by Shape-2. Proteins by Shape-1. Proteins by Composition
hapter 5: utline Amino Acids Amino acid classes Bioactive AA Modified AA Peptides Proteins (We are here) Protein structure Fibrous proteins Globular proteins tereoisomers Titration of AA AA reactions 5P2-1
More informationLesson 5 Proteins Levels of Protein Structure
Lesson 5 Proteins Levels of Protein Structure Primary 1º Structure The primary structure is simply the sequence of amino acids in a protein. Chains of amino acids are written from the amino terminus (N-terminus)
More informationUNIT 2 Amino acids and Proteins
UNIT 2 Amino acids and Proteins Significance of Proteins 1. Keep the cells and tissues growing, renewing and mending 2. Take part in some kinds of important physiological activities 3. Oxidation and supply
More informationChemistry 121 Winter 17
Chemistry 121 Winter 17 Introduction to Organic Chemistry and Biochemistry Instructor Dr. Upali Siriwardane (Ph.D. Ohio State) E-mail: upali@latech.edu Office: 311 Carson Taylor Hall ; Phone: 318-257-4941;
More information