Structure of proteins
|
|
- Collin Myron Peters
- 5 years ago
- Views:
Transcription
1 Structure of proteins Presented by Dr. Mohammad Saadeh The requirements for the Pharmaceutical Biochemistry I Philadelphia University Faculty of pharmacy
2 Structure of proteins The 20 a.a commonly found in proteins are joined together by peptide bonds. Increasing complexity of protein structure is best analyzed by considering four organizational levels, namely, primary, secondary, tertiary, and quaternary. (Figure 2.1).
3 I. Primary structure of proteins The sequence of amino acids in a protein is called the primary structure of the protein. Genetic diseases result in proteins with abnormal amino acid sequences, which cause improper folding and loss or impairment of normal function. If the primary structures of the normal and the mutated proteins are known, this information may be used to diagnose or study the disease.
4 I. Primary structure of proteins A. Peptide bond In proteins, amino acids are joined covalently by peptide bonds, which are amide linkages between the α- carboxyl group of one amino acid and the α-amino group of another. Peptide bonds are not broken by heating or high concentrations of urea. Prolonged exposure to a strong acid or base at elevated temperatures is required to hydrolyze these bonds nonenzymically.
5 I. Primary structure of proteins A.1. Naming of the peptide The free amino end (N-terminal) of the peptide chain is written to the left and the free carboxyl end (C-terminal) to the right. Therefore, 1. all amino acid sequences are read from the N- to the C-terminal end of the peptide. 2. All amino acid residues have their suffixes (-ine, -an, -ic, or -ate) changed to -yl, with the exception of the C-terminal amino acid. example, a tripeptide composed of an N-terminal valine, a glycine, and a C terminal leucine is called valylglycylleucine.
6 I. Primary structure of proteins A.2. Characteristics of the peptide bond The peptide bond has a 1. Partial double-bond character 2. shorter than a single bond, and is rigid planar. 3. Trans configuration. 4. Uncharged but polar. the configurations of the peptide bond is generally a trans bond in large part because of steric interference of the R- groups when in the cis position.
7 I. Primary structure of proteins A.3. Polarity of the peptide bond The C=O and NH groups of the peptide bond are uncharged, and neither accept nor release protons over the ph range of Usally ionized groups present in the side chains of the constituent amino acids. The C=O and NH groups of the peptide bond are polar, and are involved in hydrogen bonds, for example, in α-helices and β-sheet structures.
8 II. Secondary structure of proteins The regular arrangements of amino acids that are located near to each other in the linear sequence. These arrangements are termed the secondary structure of the polypeptide (not straight). The α helix, β-sheet, and β-bend (β-turn) are examples of secondary structures.
9 II. Secondary structure of proteins A. α-helix α-helix is the most common. - It is a spiral structure, consisting of a tightly packed, coiled polypeptide backbone core. - The side chains extending outward from the central axis to avoid interfering sterically with each other. - example, the keratins (α-helical), is related, to fibrous proteins (hair, skin) and their rigidity is determined by the number of disulfide bonds between the constituent polypeptide chains. myoglobin, is also highly α-helical.
10 II. Secondary structure of proteins A. α-helix 1. Hydrogen bonds An α-helix is stabilized by extensive hydrogen bonding between the peptidebond carbonyl oxygens and amide hydrogens. The hydrogen bonds extend up and are parallel to the spiral from the carbonyl oxygen of one peptide bond to the NH group of a peptide linkage four residues ahead in the polypeptide.
11 II. Secondary structure of proteins A. α-helix 2. Amino acid per turn Each turn of an α-helix contains 3.6 amino acids. Thus, amino acid residues spaced three or four residues apart in the primary sequence.
12 II. Secondary structure of proteins A. α-helix 3. Amino acid that disrupt an α-helix 1. Proline (secondary amino group) is not geometrically compatible with the right-handed spiral of the α-helix. 2. Large numbers of charged amino acids (for example, glutamate, aspartate, histidine, lysine, or arginine) disrupt the helix by forming ionic bonds. 3. Amino acids with bulky side chains, such as tryptophan, valine or isoleucine, that branch at the β-carbon can interfere with formation of the α- helix.
13 II. Secondary structure of proteins B. β-sheet The β-sheet is another form of secondary structure. The surfaces of β- sheets appear pleated, figure A. 1. Comparison of a β-sheet and an α- helix: β-sheets are composed of two or more peptide chains (β-strands). Note, in β-sheets the hydrogen bonds are to the polypeptide backbone (Figure A).
14 II. Secondary structure of proteins B. β-sheet 2. Parallel and antiparallel sheets: polypeptide chains that are arranged either antiparallel to each other (with the N- terminal and C-terminal ends of the β- strands alternating as shown in Figure2.7.B), or parallel to each other (with all the N-termini of the β strands together as shown in Figure C). β-sheet can also be formed by a single polypeptide chain folding back on itself (Figure2.7C). The hydrogen bonds are intrachain bonds of the β-sheet. Globular proteins, β-sheets.
15 II. Secondary structure of proteins C. β-bends (reverse turns, β-turns) β-bends reverse the direction of a polypeptide chain, helping it form a compact, globular shape and found on the surface of protein, and often include charged residues. β-bends are generally composed of four amino acids, one of which may be proline that causes a kink in the polypeptide chain. Glycine, is also found in β-bends. β-bends are stabilized by the formation of hydrogen and ionic bonds.
16 II. Secondary structure of proteins D. Nonrepetitive secondary structure The polypeptide chain is described as having a loop or coil conformation. not random, but rather simply have a less regular structure than those described above. [Note: The term random coil refers to the disordered structure obtained when proteins are denatured
17 II. Secondary structure of proteins E. Supersecondary structures (motifs) Supersecondary structures are produced by packing side chains from adjacent secondary structural elements close to each other. for example, α-helices and β-sheets that are adjacent (Figure 2.8).
18 III. Tertiary structure of globular proteins The primary structure of a polypeptide chain determines its tertiary structure. Tertiary refers both to the folding of domains and the final arrangement of domains in the polypeptide. The structure of globular proteins in aqueous solution is compact, with a high-density (close packing) of the atoms in the core of the molecule.
19 III. Tertiary structure of globular proteins A. Domains Domains are the fundamental functional, threedimensional structural and units of polypeptides. Polypeptide chains that are greater than 200 amino acids in length generally consist of two or more domains. The core of a domain is built from combinations of supersecondary structural elements (motifs). Domain has the characteristics of a small, compact globular protein that is structurally independent of the other domains in the polypeptide chain.
20 III. Tertiary structure of globular proteins B. Interactions stabilizing tertiary structure four types of interactions cooperate in stabilizing the tertiary structures of globular proteins. 1. Disulfide bonds: (Figure 2.9). Disulfide bind between two cysteines contributes to the stability of the threedimensional shape of the protein, and prevents it from becoming denatured in the extracellular environment. For example, many disulfide bonds are found in immunoglobulins that are secreted by cells.
21 III. Tertiary structure of globular proteins B. Interactions stabilizing tertiary structure 2. Hydrophobic interactions: Amino acids with nonpolar side chains tend to be located in the interior of the polypeptide (Figure 2.10). Amino acids with polar or charged side chains tend to be located on the surface in contact with the polar solvent.
22 III. Tertiary structure of globular proteins B. Interactions stabilizing tertiary structure 3. Hydrogen bonds: Alcohol groups of serine and threonine, can form hydrogen bonds with the oxygen of a carboxyl group or carbonyl group of a peptide bond (Figure 2.11). 4. Ionic interactions: Negatively charged groups, such as the carboxylate group (-COO - ) in the side chain of aspartate or glutamate, can interact with positively charged groups, such as the amino group (-NH3 + ) in the side chain of lysine (Figure 2.11).
23 IV. Quaternary structure of proteins The arrangement of single polypeptide (monomeric proteins) subunits is called the quaternary structure of the protein. Subunits are held together by noncovalent interactions, hydrogen bonds, ionic bonds, and hydrophobic interactions (see figure). Subunits function independently of each other, or may work cooperatively, as in hemoglobin.
24 Protein folding Protein folding, which occurs within the cell in seconds to minutes, involve nonrandom, ordered pathways. Peptide folds, secondary structures from driven by the hydrophobic effect these small structures combine to form larger structures. Additional events stabilize secondary structure and initiate formation tertiary structure. Finally, the peptide is fully folded, native (functional) from characterized by a low-energy state (figure 2.12)
25 Denaturation of proteins Protein denaturation results in the unfolding and disorganization the secondary and tertiary structures of proteins without the hydrolysis of peptide bonds (see figure). Denaturing agents include heat, organic solvents, mechanical mixing, strong acids or bases, detergents, and ions of heavy metals such as lead and mercury. Denaturation under ideal conditions, be reversible, therefore the protein refolds when the denaturing agent is removed. Most denaturation of proteins be disordered (irreversible). Denatured proteins are often insoluble and precipitate from solution.
26 Role of chaperones in protein folding proteins, folding is a facilitated process that requires a specialized group of proteins, 1. molecular chaperons, 2. adenosine triphosphate hydrolysis. The chaperons, also known as heat shock Proteins (Hsp) interact with the polypeptide at various stages during the folding process. Some chaperones bind hydrophobic region of an extended polypeptide and are important in keeping the protein unfolded until its synthesis is completed (for example, Hsp 70).
27 Protein misfolding Protein folding is a complex process. The deposits of misfolded proteins are associated with a number of diseases. A. Amyloid disease Misfolding of proteins may occur spontaneously, or by a mutation in a particular gene, which produces an altered protein. Abnormal proteolytic cleavage of normal protein leads to the formation of long, fibrillar protein assemblies consisting of β- pleated sheets. Accumulation of these insoluble, spontaneously aggregating proteins, called amyloids, that cause a parkinson and particularly Alzheimer disease. The amyloid plaque that accumulates in Alzheimer disease is amyloid β (Aβ), an extracellular peptide containing amino acid residues (β-pleated, nonbranching fibrils).
28 Protein misfolding Alzheimer factors 1. The Aβ that is deposited in the brain in Alzheimer disease is derived by enzymic cleavage (secretases) from the larger amyloid precursor protein, a single transmembrane protein expressed on the cell surface in the brain and other tissues (Figure 2.13). Most cases of Alzheimer disease are not genetically based, although at least 5 10% of cases are familial. 2. A biologic factor of Alzheimer disease is the accumulation of neurofibrillary tangles inside neurons. A tangled fibers is an abnormal form (hydrophosphorylated and insoluble) of the tau (τ) protein, which, in its healthy version, helps in the assembly of the microtubular structure. The defective τ appears to block the actions of its normal counterpart.
29 Protein misfolding, Alzheimer disease
30 Protein misfolding B. Prion disease Prion protein=normal protein; prion=abnormal protein (almost in brain). The prion protein (PrP) has been strongly implicated as the causative agent of transmissible spongiform encephalopathies (TSEs), including Creutzfeldt-Jakob disease in humans, scrapie in sheep, and bovine spongiform encephalopathy in cattle (popularly called mad cow disease ). the agent causing scrapie in sheep was associated with a single protein species. This infectious protein is designated PrP Sc (Sc=scrapie). PrP Sc is highly resistant to proteolytic degradation, and tends to form insoluble aggregates of fibrils, similar to the amyloid found in some other diseases of the brain.
31 Protein misfolding B. Prion disease Noninfectious PrP c contain α-helix are replaced by PrP sc β-sheets in the infectious form (Figure 2.14). PrP c + PrP sc PrP sc + PrP sc The infective agent is an altered of a normal protein, which acts as a template for converting the normal protein to the pathogenic conformation. The TSEs are invariably fatal, and no treatment is currently available that can alter this outcome.
32
SRTUCTURE 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 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 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 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 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 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 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 informationLecture 4: 8/26. CHAPTER 4 Protein Three Dimensional Structure
Lecture 4: 8/26 CHAPTER 4 Protein Three Dimensional Structure 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
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 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 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 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 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 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 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 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 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 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 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 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 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 informationI) Choose the best answer: 1- All of the following amino acids are neutral except: a) glycine. b) threonine. c) lysine. d) proline. e) leucine.
1- All of the following amino acids are neutral except: a) glycine. b) threonine. c) lysine. d) proline. e) leucine. 2- The egg white protein, ovalbumin, is denatured in a hard-boiled egg. Which of the
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 informationChapter 9. Protein Folding, Dynamics, and Structural Evolution
Chapter 9 Protein Folding, Dynamics, and Structural Evolution Proteins folding Self-assembly Primary sequence dictates three dimensional structure Folding accessory proteins Protein disulfide isomerases
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 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 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 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 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 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 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 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 informationFundamentals of Organic Chemistry CHEM 109 For Students of Health Colleges
Fundamentals of Organic Chemistry CHEM 109 For Students of Health Colleges Credit hrs.: (2+1) King Saud University College of Science, Chemistry Department CHEM 109 CHAPTER 9. AMINO ACIDS, PEPTIDES AND
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 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 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 informationGentilucci, Amino Acids, Peptides, and Proteins. Peptides and proteins are polymers of amino acids linked together by amide bonds CH 3
Amino Acids Peptides and proteins are polymers of amino acids linked together by amide bonds Aliphatic Side-Chain Amino Acids - - H CH glycine alanine 3 proline valine CH CH 3 - leucine - isoleucine CH
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 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 informationProteins. Dr. Basima Sadiq Jaff. /3 rd class of pharmacy. PhD. Clinical Biochemistry
Proteins /3 rd class of pharmacy Dr. Basima Sadiq Jaff PhD. Clinical Biochemistry a Greek word that means of first importance. It is a very important class of food molecules that provide organisms not
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 informationProteins. Bởi: OpenStaxCollege
Proteins Bởi: OpenStaxCollege Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory,
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 informationPROTEINS. Building blocks, structure and function. Aim: You will have a clear picture of protein construction and their general properties
PROTEINS Building blocks, structure and function Aim: You will have a clear picture of protein construction and their general properties Reading materials: Compendium in Biochemistry, page 13-49. Microbiology,
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 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 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 informationHuman Biochemistry Option B
Human Biochemistry Option B A look ahead... Your body has many functions to perform every day: Structural support, genetic information, communication, energy supply, metabolism Right now, thousands of
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 informationSo where were we? But what does the order mean? OK, so what's a protein? 4/1/11
So where were we? We know that DNA is responsible for heredity Chromosomes are long pieces of DNA DNA turned out to be the transforming principle We know that DNA is shaped like a long double helix, with
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 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 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 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 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 informationThe building blocks of life.
The building blocks of life. All the functions of the cell are based on chemical reactions. the building blocks of organisms BIOMOLECULE MONOMER POLYMER carbohydrate monosaccharide polysaccharide lipid
More information1.4. Lipids - Advanced
1.4. Lipids - Advanced www.ck12.org In humans, triglycerides are a mechanism for storing unused calories, and their high concentration in blood correlates with the consumption of excess starches and other
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 informationاالمتحان النهائي لعام 1122
االمتحان النهائي لعام 1122 Amino Acids : 1- which of the following amino acid is unlikely to be found in an alpha-helix due to its cyclic structure : -phenylalanine -tryptophan -proline -lysine 2- : assuming
More informationFrom Atoms to Cells: Fundamental Building Blocks. Models of atoms. A chemical connection
From Atoms to Cells: A chemical connection Fundamental Building Blocks Matter - all materials that occupy space & have mass Matter is composed of atoms Atom simplest form of matter not divisible into simpler
More informationAmino acids. (Foundation Block) Dr. Essa Sabi
Amino acids (Foundation Block) Dr. Essa Sabi Learning outcomes What are the amino acids? General structure. Classification of amino acids. Optical properties. Amino acid configuration. Non-standard amino
More informationBiology. Chapter 3. Molecules of Life. Concepts and Applications 9e Starr Evers Starr
Biology Concepts and Applications 9e Starr Evers Starr Chapter 3 Molecules of Life 2015 3.1 What Are the Molecules of Life? The molecules of life contain a high proportion of carbon atoms: Complex carbohydrates
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 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 informationبسم هللا الرحمن الرحيم
بسم هللا الرحمن الرحيم Q1: the overall folding of a single protein subunit is called : -tertiary structure -primary structure -secondary structure -quaternary structure -all of the above Q2 : disulfide
More informationWe are going to talk about two classifications of proteins: fibrous & globular.
Slide # 13 (fibrous proteins) : We are going to talk about two classifications of proteins: fibrous & globular. *fibrous proteins: (dense fibers) *Their structures are mainly formed of the secondary structure
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 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 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 informationProperties of amino acids in proteins
Properties of amino acids in proteins one of the primary roles of DNA (but far from the only one!!!) is to code for proteins A typical bacterium builds thousands types of proteins, all from ~20 amino acids
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 informationChapter 20. Proteins & Enzymes. Proteins & Enzymes - page 1
Chapter 20 Proteins & Enzymes Proteins & Enzymes - page 1 Proteins & Enzymes Part 1: Amino Acids The building blocks of proteins are -amino acids, small molecules that contain a carboxylic acid and an
More informationActivities for the α-helix / β-sheet Construction Kit
Activities for the α-helix / β-sheet Construction Kit The primary sequence of a protein, composed of amino acids, determines the organization of the sequence into the secondary structure. There are two
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 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 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 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 informationThe building blocks of life.
The building blocks of life. The 4 Major Organic Biomolecules The large molecules (biomolecules OR polymers) are formed when smaller building blocks (monomers) bond covalently. via anabolism Small molecules
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 informationProteins. These are polymers of 20 common amino acids linked in various sequences. Proteins differ in molecular mass, molecular structure and shape
Proteins These are polymers of 20 common amino acids linked in various sequences. Proteins differ in molecular mass, molecular structure and shape Characteristics if protein Amino acids are linked by covalent
More informationAMINO ACIDS STRUCTURE, CLASSIFICATION, PROPERTIES. PRIMARY STRUCTURE OF PROTEINS
AMINO ACIDS STRUCTURE, CLASSIFICATION, PROPERTIES. PRIMARY STRUCTURE OF PROTEINS Elena Rivneac PhD, Associate Professor Department of Biochemistry and Clinical Biochemistry State University of Medicine
More informationWHY IS THIS IMPORTANT?
CHAPTER 2 FUNDAMENTAL CHEMISTRY FOR MICROBIOLOGY WHY IS THIS IMPORTANT? An understanding of chemistry is essential to understand cellular structure and function, which are paramount for your understanding
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 informationBIOLOGICAL MOLECULES. Although many inorganic compounds are essential to life, the vast majority of substances in living things are organic compounds.
BIOLOGY 12 BIOLOGICAL MOLECULES NAME: Although many inorganic compounds are essential to life, the vast majority of substances in living things are organic compounds. ORGANIC MOLECULES: Organic molecules
More informationA. Lipids: Water-Insoluble Molecules
Biological Substances found in Living Tissues Lecture Series 3 Macromolecules: Their Structure and Function A. Lipids: Water-Insoluble Lipids can form large biological molecules, but these aggregations
More informationOrganic Chemistry - Problem Drill 23: Amino Acids, Peptides, and Proteins
rganic Chemistry - Problem Drill 23: Amino Acids, Peptides, and Proteins No. 1 of 10 1. Which amino acid does not contain a chiral center? (A) Serine (B) Proline (C) Alanine (D) Phenylalanine (E) Glycine
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 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 informationLesson 2. Biological Molecules. Introduction to Life Processes - SCI 102 1
Lesson 2 Biological Molecules Introduction to Life Processes - SCI 102 1 Carbon in Biological Molecules Organic molecules contain carbon (C) and hydrogen (H) Example: glucose (C 6 H 12 O 6 ) Inorganic
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 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 informationBiological Molecules
The Chemical Building Blocks of Life Chapter 3 Biological molecules consist primarily of -carbon bonded to carbon, or -carbon bonded to other molecules. Carbon can form up to 4 covalent bonds. Carbon may
More informationThe Chemical Building Blocks of Life. Chapter 3
The Chemical Building Blocks of Life Chapter 3 Biological Molecules Biological molecules consist primarily of -carbon bonded to carbon, or -carbon bonded to other molecules. Carbon can form up to 4 covalent
More informationCHY2026: General Biochemistry. Unit 4:Amino Acid Chemistry
CHY2026: General Biochemistry Unit 4:Amino Acid Chemistry http://www.hcc.mnscu.edu/programs/dept/chem/v.27/amino_acid_structure_2.jpg Hydrogen Amino group Carboxyl Group Unique side chain (R-group) R Central
More informationReactions and amino acids structure & properties
Lecture 2: Reactions and amino acids structure & properties Dr. Sameh Sarray Hlaoui Common Functional Groups Common Biochemical Reactions AH + B A + BH Oxidation-Reduction A-H + B-OH + energy ª A-B + H
More informationChapter 3. Structure of Enzymes. Enzyme Engineering
Chapter 3. Structure of Enzymes Enzyme Engineering 3.1 Introduction With purified protein, Determining M r of the protein Determining composition of amino acids and the primary structure Determining the
More informationMacromolecules. Note: If you have not taken Chemistry 11 (or if you ve forgotten some of it), read the Chemistry Review Notes on your own.
Macromolecules Note: If you have not taken Chemistry 11 (or if you ve forgotten some of it), read the Chemistry Review Notes on your own. Macromolecules are giant molecules made up of thousands or hundreds
More informationChapter 5 Overview. Amino Acids, Peptides, and Proteins. Proteins molecular tools of life. Functions
Chapter 5 Overview Amino Acids, Peptides, and Proteins Proteins molecular tools of life Functions n n n n n Structural cell shape, connective tissue (cartilage, bond) Catalysis enzymes Metabolic regulation
More informationAP BIOLOGY: READING ASSIGNMENT FOR CHAPTER 5
1) Complete the following table: Class Monomer Functions Carbohydrates 1. 3. Lipids 1. 3. Proteins 1. 3. 4. 5. 6. Nucleic Acids 1. 2) Circle the atoms of these two glucose molecules that will be removed
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 information