Proteins: Structure and Function 2/8/2017 1
|
|
- Crystal Cook
- 6 years ago
- Views:
Transcription
1 Proteins: Structure and Function 2/8/2017 1
2 outline Protein functions hemistry of amino acids Protein Structure; Primary structure Secondary structure Tertiary structure Quaternary structure 2/8/2017 2
3 Overview Proteins are the most abundant biological macromolecules, occurring in all cells and all parts of cells. They occur in great variety; thousands of different kinds, ranging in size from relatively small peptides to huge polymers with molecular weights in the millions, may be found in a single cell. Simple monomeric subunits (amino acids) provide the key to the structure of the thousands of different proteins. All proteins, whether from the most ancient lines of bacteria or from the most complex forms of life, are constructed from the same set of 20 amino acids They are the molecular instruments through which genetic information is expressed. Proteins exhibit enormous diversity of biological function and are the most important final products of the information pathways 2/8/2017 3
4 Biological Functions 1. Enzyme catalysts Almost all chemical reactions in biological systems are catalyzed by enzymes Nearly all known enzymes are proteins. 2. Transport and storage Many small molecules and ions are transported by specific proteins e.g aemoglobin transports oxygen. Iron is stored in the liver as ferritin. 3. oordinated motion Muscle contraction is accomplished by sliding motion of two kinds of protein filaments; myosin and actin 2/8/2017 4
5 4. Mechanical support Tensile strength of the skin and bone is due to the presence of collagen 5. Immune protections Antibodies and most Antigens are proteins 6. Generation and transmission of nerve impulses Receptor proteins at the nerve endplate play a role in transmission of impulses 7. ontrols growth and differentiation Growth factor proteins i.e Growth ormone coordinate activities of different cells in multicellular organisms. 2/8/2017 5
6 Properties key to their Function 1. Are linear polymers of amino acids. Protein function is directly dependent on its 3 dimensional structure which is determined by the linear sequence of amino acids in the protein polymer 2. ontain a wide range of functional groups. includes alcohols, thiols, thioethers, carboxylic acids, carboxylamides, and a variety of basic groups. When combined in various sequences, this array of functional groups accounts for the broad spectrum of protein function. E.g at active sites of enzymes. 2/8/2017 6
7 3. an interact with one another and with other biomolecules to form complex assemblies. In these assemblies proteins act synergistically to generate capabilities not afforded by the individual component proteins. These assemblies include macro-molecular machines that carry out the accurate replication of DNA, the transmission of signals within cells, and many other essential processes. 4. Some are quite rigid, whereas others display limited flexibility. Rigid units can function as structural elements in the cytoskeleton or in connective tissue. Parts of proteins with limited flexibility may act as hinges, springs, and levers that are crucial to protein function, to the assembly of proteins with one another and with other molecules into complex units, and to the transmission of information within and between cells 2/8/2017 7
8 Amino Acids: Structure Proteins are polymers of amino acids, with each amino acid residue joined to its neighbor by a specific type of covalent bond. The term residue reflects the loss of the elements of water when one amino acid is joined to another. All mammalian proteins are built from 20 amino acids. These are the one that are coded for in the genetic code. But the are more than 300 different amino acids in nature. All the 20 amino acids have an α carbon to which a carboxyl group, an amino group and a distinctive side chain (R- group) is attached. Except 2/8/2017 proline. 8
9 Amino acids: lassification 1. Non polar side chains: Aliphatic and Aromatic Do not bind, give protons, or participate in hydrogen or ionic bonds. Are important in hydrophobic interactions In proteins found in aqueous solutions, these non polar R groups cluster together in the interior of the protein. Fill up the interior of the folded protein and help give the protein its 3 D shape. Proline; the side chain and the amino group form a ring structure called an imino group. Tyrosine has a O group and can lose protons at alkaline p. O group makes tyrosine polar 2/8/2017 9
10 2/8/
11 2/8/
12 2. Uncharged Polar Side chains ave zero net charge at neutral p ysteine and Tyrosine can lose proton at alkaline p Serine, theronine and tyrosine contain O group that participate in hydrogen bonding. Asparagine and glutamine used their carbonyl and amide groups to form hydrogen bonds. ysteine form disulfide bonds when two sulfhydrl group become oxidized to form a cystine dimer Side chains are site for attachment eg O for attachment of the phosphate group. Also for attachment of oligosaccharides in glycoproteins. 2/8/
13 2/8/
14 3. Acidic side chains At neutral p, they are fully ionized; containing a negatively charged carboxyl group ( _coo-) Are proton donors at physiological p and hence are negatively charged. 2/8/
15 4. Basic side chains Are proton acceptors Lysine and arginine are fully ionized and positively charged at physiological p. But istidine is weakly basic and in proteins, it can be positively charged or neutral depending on the p. This is important in the functioning of proteins such as myoglobin. 2/8/
16 The α-r groups determine the properties of amino acids Glycine the smallest amino acid often occurs where peptides bend sharply. ydrophobic R groups of alanine, valine, leucine and isoleucine and aromatic R groups of phenylalanine, tyrosine, and tryptophan occur primarily in the interior of cytosolic proteins. Proline often found on bends of folded proteins. The charged R groups of basic and acidic amino acids stabilize specific protein conformation via ionic interactions, or salt bonds. istidine plays an important role in enzymatic catalysis. 2/8/
17 Functional groups dictate the chemical reactions of amino acids Each functional group of an amino acid exhibits all its characteristic chemical reactions; For carboxylic acid groups : formation of esters, amides and acid anhydrides For amino groups acylation, amidation and esterification For O and S groups oxidation and esterification The most important reaction of amino acids is the formation of peptide bonds 2/8/
18 Amino acids are linked by peptide bonds to form polypeptide chains + 3 N R 2 R 2 R 1 O O O O N 3 N N 2 O O O O R 1 Peptide bond 2/8/
19 Two amino acids may be joined by a peptide bond to form a dipeptide Three two peptide bonds to form a tripeptide Peptides with more than 10 amino acid residues are termed polypeptides and when few amino acids are joined, peptides are referred to as oligopeptides -An amino acid unit in a chain is a residue -By conversion the amino end is taken to be the beginning of a polypeptide chain. O Aminoterminal end O N + 3 O N O N O N O O arboxyterminal end The tetrapeptide with seryltyrosylalanylleucine or Ser-Tyr-Ala-Leu 2/8/
20 - A polypeptide chain consists of a regularly repeating part, the main chain (backbone) and a variable part consisting of distinctive side chains (R 1, R 2 and R 3 R 1 O R 2 O R 3 O N N N Amino acid sequence determines the primary structure -Amino acids present in peptides are termed aminoacyl residues - the suffixes ate or ine are replaced with -yl (eg alanyl, aspartyl, tyrosyl) - peptides are named as derivatives of the carboxyl terminal aminoacyl residue (eg lysyl-leucyl-tyrosyl-glutamine). The ine ending of glutamine indicates that the carboxyl group is not involved in peptide bond formation 2/8/
21 Some proteins contain chemical groups other than amino acids Simple proteins contain only amino acid residues and no other chemical groups onjugated proteins contain permanently associated chemical groups in addition to amino acids The non amino acid part of a conjugated protein is called the prosthetic group - onjugated proteins are classified on the basis of the chemical nature of the prosthetic group -lipoproteins contain lipid -glycoproteins contain sugar groups -metalloproteins contain a specific metal -Usually the prosthetic group plays a role in the protein s biological activity A protein without its characteristic prosthetic group is termed as apoprotein 2/8/
22 Levels of Protein Structure Primary structure A description of all covalent bondss (mainly peptide bonds and disulfide bonds) linking amino acid residues in a polypeptide chain. The most important element of the primary structure is its amino acid sequence which determines; how a protein folds up into its unique three-dimensional structure and this in turn determines the function of the protein cellular location certain sequences serve as signals that target proteins for export or tissue distribution Attachment sites for prosthetic groups an also elucidate evolutionary trees
23 Types of non covalent bonds in primary structure; 1. ydrogen Bonds 2. ydrophobic interactions 3. Electrostatic (Ionic) Bonds
24 Protein Secondary structure Is a stable arrangement of amino acid residues giving rise to recurring structural patterns The α helix is a common protein secondary structure The simplest structure the polypeptide chain can assume with its rigid peptide bonds (other bonds free to rotate) is a helical structure The helix is stabilized by hydrogen bonds between the N and O groups of the main chain The O group of each amino acid is hydrogen bonded to the N group of the amino acid that is located four residues ahead in the linear sequence All the main chain N and O groups are hydrogen bonded (except those close to each end of the helix)
25 O O N R 1 O N R 2 N R 3 O N R 4 N R 5 O In the α-helix the O group of residue n is hydrogen bonded to the N group of the residue (n+ 4) The helix can be right handed (counter clock wise) or left handed (clock wise) The α- helices found in protein are right-handed
26 The β-pleated sheets -The pleated sheet is extended into a zig zag (pleated) formation rather the being tightly coiled as in the α helix. - the β pleated sheet is stabilized by hydrogen bonds between N and O groups in different polypeptide strands where as in the α helix the hydrogen bonds between N and O groups are on the same strand. -R groups of adjacent amino acids protrude from the zigzag structure in opposite directions
27 Adjacent chains in a β pleated sheet can run in the same direction (parallel β sheet) or in the opposite direction (antiparallel β sheet) Individual segments that form a β sheet are: usually nearby on a polypeptide chain can be distant from each other in the linear sequence of the polypeptide they may be segments in different polypeptide chains
28 Supersecondary structure Refers to clusters of secondary structures -Eg a β strand separated from another β strand by an α helix to form a motif (β-α-β unit) -Such motifs are intermediate between secondary and tertiary structures
29 Protein structure showing α-helix and β sheet conformations α-helix β sheets Random coils
30 Protein Tertiary Structure -Refers to the entire three dimensional conformation of a polypeptide - - In contrast to secondary structure which refers to the spatial arrangement of amino acid residues that are adjacent in the primary structure, tertiary structures include longer - range aspects of amino acid sequence -It indicates in three-dimensions how secondary structural features - helices, sheets, bends, turns and loops - assemble to form domains and how these domains relate spatially to one another -A domain is a section of protein structure able to perform a particular chemical or physical task such as binding to substrate -other domains may - anchor a protein to a substrate - interact with a regulatory molecule
31 Protein Quaternary Structure Quaternary structure comprises 2 or more polypeptide chains united by forces other than covalent bonds ( ie not peptide or disulfide bonds) -The forces that stabilize these aggregates are hydrogen bonds and electrostatic bonds formed between residues on the surface of the polypeptide chains -Such proteins are called oligomers and the individual polypeptides of which they are composed are protomers ( monomers,or subunits) 31
32 -Two major groups -Fibrous proteins - polypeptide chains arranged in long strands or sheets -Usually consist largely of a single type of secondary structure -Provide support, shape and external protection to vertebrates -Insoluble in water due to a high concentration of hydrophobic amino acids both in the interior of the protein and on its surface -eg α-keratin, collagen etc - Globular proteins polypeptide chains folded into spherical or globular shape -Often contain several types of secondary structure -Most enzymes, regulatory proteins, immunoglobulin, transport proteins, motor proteins are globular proteins play a special role in intracellular regulation because the protomers can assume different spatial arrangement relative to each other with resulting changes in the properties of the oligomer eg haemoglobin 32
Proteins 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 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 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 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 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 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 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 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 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 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 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 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 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 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 consist in whole or large part of amino acids. Simple proteins consist only of amino acids.
Today we begin our discussion of the structure and properties of proteins. Proteins consist in whole or large part of amino acids. Simple proteins consist only of amino acids. Conjugated proteins contain
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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 informationBielkoviny, enzýmy. Július Cirák. Protein Structure Timothy G. Standish
Bielkoviny, enzýmy Július irák Alanine Acid Different Amino Acid lasses 2 on-polar Aspartic acid 2 Amine Generic 2? R Acid Basic Polar istidine 2 S 2 + ysteine Levels f Protein rganization Primary Structure
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 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 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 informationDifferent levels of protein structure
Dr. Sanjeeva Srivastava Proteins and its function Amino acids: building blocks Different levels of protein structure Primary, Secondary, Tertiary, Quaternary 2 Proteomics ourse PTEL 1 Derived from Greek
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 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 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 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 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 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 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 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 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 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 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 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 information3150:112 SAMPLE TEST 2. Print out a copy Answer the questions on your own. Check the answers at GOBC Ans.pdf. Good Luck!
SAMPLE TEST 2 3150:112 Print out a copy Answer the questions on your own. Check the answers at GOBC Ans.pdf. Good Luck! QUESTIONS 1-3 REFER TO TE FOLLOWING: A. C 2 O O B. C 2 O O O C 2 O C. O C 2 O 1.
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 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 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 informationDifferent types of proteins. The structure and properties of amino acids. Formation of peptide bonds.
Introduction to proteins and amino acids Different types of proteins. The structure and properties of amino acids. Formation of peptide bonds. Introduction We tend to think of protein as a mass noun: a
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 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 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 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 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 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 informationLecture 4. Grouping Amino Acid 7/1/10. Proteins. Amino Acids. Where Are Proteins Located. Nonpolar Amino Acids
Proteins Lecture 4 Proteins - Composition of Proteins (Amino Acids) Chapter 21 ection 1-6! Proteins are compounds of high molar mass consisting almost entirely of amino acid chain(s)! Molar masses range
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 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 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 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 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 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 informationHonors Biology Chapter 3: Macromolecules PPT Notes
Honors Biology Chapter 3: Macromolecules PPT Notes 3.1 I can explain why carbon is unparalleled in its ability to form large, diverse molecules. Diverse molecules found in cells are composed of carbon
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 informationPAPER No. : 16, Bioorganic and biophysical chemistry MODULE No. : 22, Mechanism of enzyme catalyst reaction (I) Chymotrypsin
Subject Paper No and Title 16 Bio-organic and Biophysical Module No and Title 22 Mechanism of Enzyme Catalyzed reactions I Module Tag CHE_P16_M22 Chymotrypsin TABLE OF CONTENTS 1. Learning outcomes 2.
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 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 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 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 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 informationMaha AbuAjamieh. Tamara Wahbeh. Mamoon Ahram
12 Maha AbuAjamieh Tamara Wahbeh Mamoon Ahram - - Go to this sheet s last page for definitions of the words with an asterisk above them (*) - You should memorise the 3-letter abbreviations, of all the
More informationCHM333 LECTURE 6: 1/25/12 SPRING 2012 Professor Christine Hrycyna AMINO ACIDS II: CLASSIFICATION AND CHEMICAL CHARACTERISTICS OF EACH AMINO ACID:
AMINO ACIDS II: CLASSIFICATION AND CHEMICAL CHARACTERISTICS OF EACH AMINO ACID: - The R group side chains on amino acids are VERY important. o Determine the properties of the amino acid itself o Determine
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 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 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 informationChapter 20. Protiens. Chapter 21. Protein and the Amino Acids. These are biopolymers that are constructed from a limited set of amino acids.
hemistry 121(01) Winter 2009-10 Introduction to rganic hemistry and Biochemistry Instructor Dr. Upali Siriwardane (Ph.D. hio State) E-mail: upali@chem.latech.edu ffice: 311 arson Taylor all ; Phone: 318-257-4941;
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 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 informationTala Saleh. Tamer Barakat. Diala Abu-Hassan
13 Tala Saleh Tamer Barakat Diala Abu-Hassan Biochemical application of monosodium glutamate MSG MSG is a glutamic acid derivative, used as a flavor enhancer in Asian food. Chinese restaurant syndrome
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 informationthe nature and importance of biomacromolecules in the chemistry of the cell: synthesis of biomacromolecules through the condensation reaction lipids
the nature and importance of biomacromolecules in the chemistry of the cell: synthesis of biomacromolecules through the condensation reaction lipids and their sub-units; the role of lipids in the plasma
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 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 informationReview of Biochemistry
Review of Biochemistry Chemical bond Functional Groups Amino Acid Protein Structure and Function Proteins are polymers of amino acids. Each amino acids in a protein contains a amino group, - NH 2,
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 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 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 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 informationLecture 11 AMINO ACIDS AND PROTEINS
Lecture 11 AMINO ACIDS AND PROTEINS The word "Protein" was coined by J.J. Berzelius in 1838 and was derived from the Greek word "Proteios" meaning the first rank. Proteins are macromolecular polymers composed
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 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 informationCOO - l. H 3 N C a H l R 1
COO - l + H 3 N C a H l R 1 Amino acids There are 20 standard amino acids. All proteins are built from the same amino acids. The most important criteria for classification is affinity to water: hydrophilic
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 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 information