BIO 311C Spring Lecture 15 Friday 26 Feb. 1
|
|
- Georgia Bennett
- 5 years ago
- Views:
Transcription
1 BIO 311C Spring 2010 Lecture 15 Friday 26 Feb. 1
2 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 other modifications 3 Functional Protein
3 Structural Formula of an Amino Acid central carbon atom A single amino acid that is not chemically attached to anything else is called a "free amino acid". Characteristics of Free Amino Acids A central carbon atom is attached to four chemical groups. The central carbon is an asymmetric carbon atom unless R is identical to one of the other three chemical groups. Both the amino and the carboxylic acid functional group of free amino acids are ionized at near neutral ph. 4
4 Ways of Showing the Structural Formula of an Amino Acid Uncharged form; does not occur in aqueous solutions at neutral ph. Charged form that occurs in aqueous solutions at near neutral ph. Detailed structure Abbreviated Structure 5
5 Amino Acids Used to Construct Proteins central carbon atom H + H 3 N C COO - Twenty different kinds of amino acids are used for constructing proteins, each with a different "R" group. R Since the central carbon atom of an amino acid is asymmetrical, there are 2 enantiomers of each kind of amino acid. Cells use only the "L" enantiomer of each kind of amino acid to construct proteins. The R-group of a few kinds of amino acids carry an amino or a carboxylic acid functional group. These amino acids carry three electrical charges at ph values near 7. 6
6 Aspartic Acid (shown without its functional groups ionized) Glycine (shown without its functional groups ionized) Threonine (shown without its functional groups ionized) How many electric charges would this free amino acid have in the cytoplasmic matrix of a living cell? How many asymmetric carbon atoms does this free amino acid contain? How many electric charges would this free amino acid have in the cytoplasmic matrix of a living cell? How many asymmetric carbon atoms does this free amino acid contain? How many electric charges would this free amino acid have in the cytoplasmic matrix of a living cell? How many asymmetric carbon atoms does this free amino acid contain? 7
7 Formation of a Peptide Bond from Two Amino Acids These atoms are lost as a molecule of water during the formation of a peptide bond. These atoms are covalently bonded together during formation of a peptide bond In most cases R 1 and R 2 will not be the same chemical structures. 8
8 Dipeptide Formation From Two Amino Acids + aa 1 + aa 2 H 2 O dehydration reaction dipeptide + H 2 O 9 Atoms of peptide bond
9 A Peptide Bond Between Two Amino Acids A peptide bond between two amino acids consists of the four atoms shown at right. All 6 atoms shaded in grey (above) lie in the same rigid plane, with the double-bonded oxygen projecting in the opposite direction from the hydrogen atom that is bonded to the nitrogen atom. O C N H 10 The carboxylic acid and amino functional groups that formed the peptide bond (see previous slide) can no longer ionize after they have become incorporated into a peptide bond.
10 Oligopeptides and Polypeptides dipeptide: Two amino acids covalently bonded together by a peptide bond: oligopeptide: 3-20 amino acids covalently bonded together by peptide bonds tripeptide: Three amino acids covalently bonded together by two peptide bonds tetrapeptide: Four amino acids covalently bonded together by three peptide bonds polypeptide (also called a polypeptide chain): More than twenty amino acids covalently bonded together by peptide bonds 11
11 Oligopeptides and polypeptides have two distinct ends: - an N-terminal end (also called an amino-terminal end, - a C-terminal end (also called a carboxy-terminal end). Example N-terminal end + H 3 N H C O C N H C C H N COO C-terminal end - R 1 H R 2 O A tripeptide Can you identify the peptide bonds in this molecule? 12
12 Hydrogen Bonding Between Two Peptide Groups Direction of polypeptide chain N-terminal end hydrogen bond C-terminal end Direction of polypeptide chain 13 The structure imposed on portions of a polypeptide chain due to hydrogen bonding between different peptide bonds is called the secondary structure of the polypeptide chain.
13 Multiple hydrogen bonds can form between adjacent peptide groups along the folded polypeptide chain Direction of polypeptide chain N-terminal end additional hydrogen bond hydrogen bond C-terminal end Direction of polypeptide chain 14
14 A common secondary structure of polypeptide chains resembles the shape of a stretched spring and is called the alpha-helix conformation. Abbreviated illustration showing back-bone structure and ribbon diagram of a portion of a polypeptide chain in an α-helix conformation. Illustration showing all atoms of a portion of a polypeptide chain in an α-helix conformation. Yellow lines represent hydrogen bonds. This conformation is stabilized by multiple hydrogen 15 bonds between atoms of different peptide bonds.
15 Another common secondary structure of polypeptide chains resembles the shape of a sheet of paper folded back and forth; it is called the betasheet (or pleated sheet or beta pleated sheet) conformation. Illustration showing back-bone structure and diagram of two portions of a polypeptide chain that are aligned together in a pleated sheet conformation. The polypeptide chain may fold back again to allow three (or more) regions of the polypeptide chain to align in a thicker pleated sheet conformation. Note the oxygen and hydrogen atoms of peptide bonds that are projecting out such that they are available to form additional hydrogen bonds, which would expand the pleated sheet. The R groups actually project at approximately right angles to the plane of the pleated sheet. As with the alpha-helix conformation, the pleated-sheet conformation is 16 stabilized by hydrogen bonding between atoms of different peptide bonds.
16 Categories of R Groups that Occur in Amino Acids I. No R-group (glycine contains only H) II. With R-group A. Nonpolar R-Group B. Polar R-Group 1. non-ionized 2. ionized a. cationic b. anionic generalized amino acid 18
17 Leucine an amino acid with a nonpolar R-group Serine an amino acid with a polar, non-charged R-group R-groups are shown with a light pink background. 19
18 Lysine an amino acid with a cationic R-group Aspartic acid an amino acid with an anionic R-group 20 R-groups are shown with a light pink background.
19 The Amino Acid Sequence of a Polypeptide Chain From textbook Fig. 5.21, p. 82 Each living cell produces several thousands of different kinds of polypeptide chains. Each kind of polypeptide chain has an exact number of amino acids. The sequence of amino acids is exactly the same for each copy of the same kind of polypeptide chain. Some Features of This Specific Polypeptide Chain It consists of 127 amino acids. Its N-terminal amino acid is Gly (G). Its C-terminal amino acid is Glu (E). Amino acid number 25 is Ala (A). The amino acids of a polypeptide chain are numbered sequentially, starting from the N-terminal (aminoterminal) end. 21
20 Representation of a the Primary Structure of a Portion of a Specific Polypeptide Chain amino acids peptide bonds H + 3 N COO - Ala A Asp D Gly G Phe F Leu L Lys K Ser S Cys C Dotted line indicates that the polypeptide chain continues. Dotted line indicates that the polypeptide chain continues. Previously amino acids were given three-letter abbreviated names; Now they are usually designated by one-letter abbreviated names. The specific sequence of amino acids along a polypeptide chain, starting at the N-terminal end, is called the primary structure of the polypeptide chain. 22 In general the sequence is not a regular, repeating pattern. It is unique to each different kind of polypeptide chain.
21 Secondary Structures Contribute to the Overall Size and Shape of a Polypeptide Chain From Textbook Fig. 5.19, p. 81 An alpha-helix secondary structure A beta-sheet secondary structure Each alpha helix and each beta (pleated) sheet contributes to only a portion of the overall threedimensional shape of the polypeptide chain. 23
22 Examples of Specific R-groups Along a Region of a Polypeptide Chain one-letter amino acid identifier backbone of Polypeptide chain R-groups of amino acids The differing R-groups on different amino acids carry functional groups that confer specific properties to each amino acid positioned along the polypeptide chain. Some R groups along the polypeptide chain are nonpolar, some are polar and uncharged, some are positively charged, and some are negatively charged. 24
23 Kinds of Bonds that May Form Between Different R-Groups When a Polypeptide Chain Bends and Folds in Various Ways From textbook Fig. 5.21, p 83 Covalent bond (Disulfide bond) Polar bonds Hydrogen bonds Electrovalent (ionic) bonds Hydrophobic bonding 25
24 From Fig. 5.19, p. 81, of textbook α helix Representations of the Conformation of a Functional Polypeptide Chain β sheet disulfide Ribbon model lysozyme Space-filling model 26 The three-dimensional shape (conformation) of a polypeptide chain is called its tertiary structure. The secondary structure and tertiary structure of a polypeptide chain are determined by its primary structure. Thus, each different polypeptide chain with its unique sequence of amino acids also has its own unique conformation.
25 A ribbon structure of ribonuclease is shown, illustrating its native conformation. Ribonuclease serves as a functional enzyme when in this conformation. Ribonuclease A polypeptide chain that is folded into its normal, functional conformation is said to be in its native conformation. 27 A polypeptide that is folded improperly so that it cannot function is said to be to be denatured or in a denatured conformation.
26 Relationship Between a Protein and a Polypeptide Chain A polypeptide chain is a sequence of 20 or more amino acids held together by peptide bonds. When one or more polypeptide chains are folded in a conformation that forms a functional unit, then the unit is called a protein (or an active protein). Thus, all proteins contain at least one polypeptide chain. 28
27 Monomeric and Oligomeric Proteins α-tubulin β-tubulin lysozyme is a monomeric protein 29 tubulin is a dimeric protein A protein that consists of only one polypeptide chain is called a monomeric protein. A protein that consists of several (2 or a few) polypeptide chains is called an oligomeric protein. The three-dimensional shape of an oligomeric protein is called its quaternary structure. The individual polypeptide chains of an oligomeric protein are called subunits of the protein. Microtubules are polymeric proteins
BIOB111 - 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 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 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 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 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 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 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 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 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 informationPractice Problems 3. a. What is the name of the bond formed between two amino acids? Are these bonds free to rotate?
Life Sciences 1a Practice Problems 3 1. Draw the oligopeptide for Ala-Phe-Gly-Thr-Asp. You do not need to indicate the stereochemistry of the sidechains. Denote with arrows the bonds formed between 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 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 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 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 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 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 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 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 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 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 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 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 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 informationKEY NAME (printed very legibly) UT-EID
BIOLOGY 311C - Brand Spring 2007 KEY NAME (printed very legibly) UT-EID EXAMINATION II Before beginning, check to be sure that this exam contains 7 pages (including front and back) numbered consecutively,
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 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 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 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 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 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 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 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 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 informationBiochemistry - I. Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture 1 Amino Acids I
Biochemistry - I Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology, Kharagpur Lecture 1 Amino Acids I Hello, welcome to the course Biochemistry 1 conducted by me Dr. S Dasgupta,
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 informationFor questions 1-4, match the carbohydrate with its size/functional group name:
Chemistry 11 Fall 2013 Examination #5 PRACTICE 1 ANSWERS For the first portion of this exam, select the best answer choice for the questions below and mark the answers on your scantron. Then answer the
More informationFor questions 1-4, match the carbohydrate with its size/functional group name:
Chemistry 11 Fall 2013 Examination #5 PRACTICE 1 For the first portion of this exam, select the best answer choice for the questions below and mark the answers on your scantron. Then answer the free response
More informationMITOCW MIT7_01SCF11_track13_300k.mp4
MITOCW MIT7_01SCF11_track13_300k.mp4 HAZEL SIVE: All right. Let's move on to the second topic of our discussion today, which we will start today and then continue on Friday. And this is a discussion of
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 informationChapter 3: Amino Acids and Peptides
Chapter 3: Amino Acids and Peptides BINF 6101/8101, Spring 2018 Outline 1. Overall amino acid structure 2. Amino acid stereochemistry 3. Amino acid sidechain structure & classification 4. Non-standard
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 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 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 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 informationBiochemistry Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology Kharagpur. Lecture -02 Amino Acids II
Biochemistry Prof. S. Dasgupta Department of Chemistry Indian Institute of Technology Kharagpur Lecture -02 Amino Acids II Ok, we start off with the discussion on amino acids. (Refer Slide Time: 00:48)
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 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 informationChapter 5: Structure and Function of Macromolecules AP Biology 2011
Chapter 5: Structure and Function of Macromolecules AP Biology 2011 1 Macromolecules Fig. 5.1 Carbohydrates Lipids Proteins Nucleic Acids Polymer - large molecule consisting of many similar building blocks
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 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 information9/6/2011. Amino Acids. C α. Nonpolar, aliphatic R groups
Amino Acids Side chains (R groups) vary in: size shape charge hydrogen-bonding capacity hydrophobic character chemical reactivity C α Nonpolar, aliphatic R groups Glycine (Gly, G) Alanine (Ala, A) Valine
More informationCHAPTER 29 HW: AMINO ACIDS + PROTEINS
CAPTER 29 W: AMI ACIDS + PRTEIS For all problems, consult the table of 20 Amino Acids provided in lecture if an amino acid structure is needed; these will be given on exams. Use natural amino acids (L)
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 informationLecture 3: 8/24. CHAPTER 3 Amino Acids
Lecture 3: 8/24 CHAPTER 3 Amino Acids 1 Chapter 3 Outline 2 Amino Acid Are Biomolecules and their Atoms Can Be Visualized by Two Different Ways 1) Fischer projections: Two dimensional representation of
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 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 informationLipids: diverse group of hydrophobic molecules
Lipids: diverse group of hydrophobic molecules Lipids only macromolecules that do not form polymers li3le or no affinity for water hydrophobic consist mostly of hydrocarbons nonpolar covalent bonds fats
More informationBio Factsheet. Proteins and Proteomics. Number 340
Number 340 Proteins and Proteomics Every living thing on the planet is composed of cells, and cells in turn are made of many types of molecules, including the biological molecules carbohydrates, lipids,
More information2. Which of the following is NOT true about carbohydrates
Chemistry 11 Fall 2011 Examination #5 For the first portion of this exam, select the best answer choice for the questions below and mark the answers on your scantron. Then answer the free response questions
More information3. AMINO ACID AND PEPTIDES
3. AMINO ACID AND PEPTIDES 3.1 Amino Acids and Peptides General structure - Only 20 amino-acids are found in proteins - Amino group and carboxyl group - α-carbon and side chain group 3.1 Amino Acids and
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 informationIntroduction to Protein Structure Collection
Introduction to Protein Structure Collection Teaching Points This collection is designed to introduce students to the concepts of protein structure and biochemistry. Different activities guide students
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 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 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 informationT.Y.B.Sc. SemIII Paper VI CH-336C Introduction to Biochemistry and Molecular Biology. Lecture Notes
Lecture Notes Chapter-I: Amino Acids and Proteins 1. Introduction Amino acids are biologically important organic compounds containing amine (-NH 2 ) and carboxylic acid (-COOH) functional groups, usually
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 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 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 informationAmino Acids. Lecture 4: Margaret A. Daugherty. Fall Swiss-prot database: How many proteins? From where?
Lecture 4: Amino Acids Margaret A. Daugherty Fall 2004 Swiss-prot database: How many proteins? From where? 1986 Use http://us.expasy.org to get to swiss-prot database Proteins are the workhorses of the
More information1-To know what is protein 2-To identify Types of protein 3- To Know amino acids 4- To be differentiate between essential and nonessential amino acids
Amino acids 1-To know what is protein 2-To identify Types of protein 3- To Know amino acids 4- To be differentiate between essential and nonessential amino acids 5-To understand amino acids synthesis Amino
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 informationProteins are sometimes only produced in one cell type or cell compartment (brain has 15,000 expressed proteins, gut has 2,000).
Lecture 2: Principles of Protein Structure: Amino Acids Why study proteins? Proteins underpin every aspect of biological activity and therefore are targets for drug design and medicinal therapy, and in
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 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 informationMoorpark College Chemistry 11 Fall Instructor: Professor Gopal. Examination # 5: Section Five May 7, Name: (print)
Moorpark College Chemistry 11 Fall 2013 Instructor: Professor Gopal Examination # 5: Section Five May 7, 2013 Name: (print) Directions: Make sure your examination contains TEN total pages (including this
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 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 informationBiology. Lectures winter term st year of Pharmacy study
Biology Lectures winter term 2008 1 st year of Pharmacy study 3 rd Lecture Chemical composition of living matter chemical basis of life. Atoms, molecules, organic compounds carbohydrates, lipids, proteins,
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 informationAdditional problems: 1. Match and label the conjugate acid and base pairs in the following reactions. Which one of these systems is a good buffer?
1 ESA Biochemistry Fall 2001 eview problems for the first exam Acid/Base chemistry Sections to review: 10.2,.3,.4,.6.9,.12,.13 omplete the following sentences 1. 2 3 is a acid. 2. The anion of a weak acid
More information(65 pts.) 27. (10 pts.) 28. (15 pts.) 29. (10 pts.) TOTAL (100 points) Moorpark College Chemistry 11 Spring Instructor: Professor Gopal
Moorpark College Chemistry 11 Spring 2012 Instructor: Professor Gopal Examination # 5: Section Five May 1, 2012 Name: (print) GOOD LUCK! Directions: Make sure your examination contains TWELVE total pages
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. 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 informationCHAPTER 21: Amino Acids, Proteins, & Enzymes. General, Organic, & Biological Chemistry Janice Gorzynski Smith
CHAPTER 21: Amino Acids, Proteins, & Enzymes General, Organic, & Biological Chemistry Janice Gorzynski Smith CHAPTER 21: Amino Acids, Proteins, Enzymes Learning Objectives: q The 20 common, naturally occurring
More informationPage 8/6: The cell. Where to start: Proteins (control a cell) (start/end products)
Page 8/6: The cell Where to start: Proteins (control a cell) (start/end products) Page 11/10: Structural hierarchy Proteins Phenotype of organism 3 Dimensional structure Function by interaction THE PROTEIN
More informationاستاذ الكيمياءالحيوية
قسم الكيمياء الحيوية د.دولت على سالمه استاذ الكيمياءالحيوية ٢٠١٥-٢٠١٤ الرمز الكودي : ٥١٢ المحاضرة األولى ١ Content : Definition of proteins Definition of amino acids Definition of peptide bond General
More informationOrganic molecules are molecules that contain carbon and hydrogen.
Organic Chemistry, Biochemistry Introduction Organic molecules are molecules that contain carbon and hydrogen. All living things contain these organic molecules: carbohydrates, lipids, proteins, and nucleic
More informationStructure of -amino acids. Stereoisomers of -amino acids. All amino acids in proteins are L-amino acids, except for glycine, which is achiral.
amino acids Any of a large number of compounds found in living cells that contain carbon, oxygen, hydrogen, and nitrogen, and join together to form proteins. Amino acids contain a basic amino group (NH
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 informationChapter 2. Chemical Composition of the Body
Chapter 2 Chemical Composition of the Body Carbohydrates Organic molecules that contain carbon, hydrogen and oxygen General formula C n H 2n O n -ose denotes a sugar molecule Supply energy Glucose Complex
More informationAP Biology. Proteins. Proteins. Proteins. Amino acids H C OH H R. Effect of different R groups: Polar amino acids polar or charged & hydrophilic
Most structurally & functionally diverse group : involved in almost everything enzymes (pepsin, DNA polymerase) structure (keratin, collagen) carriers & transport (, aquaporin) cell communication signals
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 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 informationA look at macromolecules (Text pages 38-54) What is the typical chemical composition of a cell? (Source of figures to right: Madigan et al.
A look at macromolecules (Text pages 38-54) What is the typical chemical composition of a cell? (Source of figures to right: Madigan et al. 2002 Chemical Bonds Ionic Electron-negativity differences cause
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 informationDerived copy of Proteins *
OpenStax-CNX module: m65486 1 Derived copy of Proteins * Martha Smith-Caldas Christopher Herren Based on Proteins by OpenStax This work is produced by OpenStax-CNX and licensed under the Creative Commons
More information