Activities for the α-helix / β-sheet Construction Kit
|
|
|
- Eugene Dennis Hoover
- 6 years ago
- Views:
Transcription
1 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 periodic secondary structure motifs, α-helix and β-sheet. Proteins can be composed of primarily α-helices (for example, β-globin) or β-sheets (for example, GFP), or a combination of the two structural motifs. The construction kits allow students to interact with these secondary structures to explore similarities and differences between the two types. Teaching Points: Each amino acid is similar, but different. The backbone of the amino acid is the same, but the sidechain (R group) is different. The unique identity of each amino acid is determined by the structure of the sidechain (R group). Sidechains have specific chemical properties determined by the chemical composition of the group. There are two repeating secondary structure motifs: α-helix and β-sheet. The secondary structure is dependent on phi-psi angles of the backbone peptide pieces. Activities for the α-helix/β-sheet Construction Kit Page 1 of 5
2 Separating Backbone Pieces Please note that there are two separate construction kits included in this collection: an α-helix kit and a β-sheet kit. In order to keep them separate, we have marked the α- carbon of the α-helix and β-sheet pieces differently. Depending on the set you received, there will be a green A (for antiparallel ) on the β-sheet and the α-helix will be blank, or there will be a green dot on the α-helix pieces and a yellow dot on the β-sheet pieces. The amino acid backbones have different phi and psi bond angles depending on whether they are a part of the α-helix or β-sheet construction kit. These angles are necessary to build either a helix or a sheet. If you notice that neither the alpha helix nor the beta sheet can be built, then the backbone pieces are probably mixed together. When you are putting the kits back into the suitcase, please make sure that the backbone pieces have been properly separated. Thank you. Copyright Center for BioMolecular Modeling. All rights reserved. Revised 11/12
3 I. Backbone Pieces There are two versions of the α-helix / β-sheet construction kit. Blank/Green A (antiparallel) Green/Yellow Dots A. Examine one α-helix backbone piece and one β-sheet backbone piece (there is an A or a yellow dot located on the backbone α-carbon atom of the β-sheet piece.) 1. How are the two pieces similar? 2. How are the two pieces different? B. The backbone pieces are colored with CPK coloring: Carbon (gray) Oxygen (red) Nitrogen (blue) 1. Draw the chemical structure of the backbone model. 2. Identify the α-carbon. What bonds to the α-carbon? 3. What part of the amino acid structure is missing in this representation? C. Examine the orientation of the angle formed by the bond between the nitrogen and the α-carbon and the bond between the α-carbon and the carbonyl-carbon in each backbone piece. 1. How are these angles different? 2. Why are the angles important for building secondary structure? Activities for the α-helix/β-sheet Construction Kit Page 2 of 5
4 II. Building an α-helix or a β-sheet A. Build an α-helix and a β-sheet without any sidechains and without any hydrogen bonds. Examine the two secondary structures. 1. What similarities are present between the two structures? 2. What differences are present between the two? 3. How is the amino-group of one amino acid positioned in relation to other amino groups? The carboxyl carbons? B. Add the hydrogen bonds to the structure. 1. Where do hydrogen bonds form within each secondary structure? 2. What function do these bonds have on the overall structure? C. Measure the length of ten amino acids in an α-helix and ten amino acids in a β-sheet (two strands of five amino acids). 1. Which secondary structure is longer? 2. Why? 3. What impact might this difference have on the structure/shape of the protein? D. Mix the two types of backbone pieces together and build a structure. 1. Were you able to successfully build a secondary structure? 2. Why or why not? Activities for the α-helix/β-sheet Construction Kit Page 3 of 5
5 III. The Unique Identity of Each Amino Acid is Determined by the Chemical Composition of the Sidechain (R Group) There are 20 amino acids that serve as the building blocks of proteins. Each amino acid has the same backbone (NH 2 -CHR- COOH). The identity of the amino acids is determined by the chemical composition of the R group. We can group the sidechains according to chemical properties, such as hydrophobic (non-polar) versus hydrophilic (polar). A. Exploring the Sidechains There are 30 sidechains in each kit. There are multiple copies of several amino acids. 1. Which amino acids have two copies? 2. Which amino acids have three copies? 3. Which amino acid has four copies? 4. Which amino acid is not included in this selection of sidechains? 5. Why do you think this amino acid is not included? B. Examine each amino acid. 1. Based on the chemical nature of each sidechain, how can you organize these sidechains into groups? 2. What similarities/differences do you see between a. Tyrosine and phenylalanine b. Serine and threonine c. Glutamine and glutamic acid d. Asparagines and aspartic acid e. Leucine and isoleucine f. Valine and leucine g. Alanine and valine h. Methionine and cysteine i. Lysine and arginine j. Tryptophan and phenylalanine k. Histidine and tryptophan 3. Looking at your structures of the α-helix and the β-sheet, which sidechains do you think would be better suited for each type of secondary structure? Activities for the α-helix/β-sheet Construction Kit Page 4 of 5
6 IV. Putting it Together A. Create a tetra-peptide using the backbone pieces (either the α-helix or the β-sheet) and sidechains. 1. Draw the chemical structure of your tetra-peptide. 2. Identify the peptide bond on your drawing. 3. Identify the sidechain (R group) on your drawing. B. Modeling Helix A of the β-globin Protein (please see the handout that accompanies the α-helix/β-sheet Collection) C. Modeling β-sheet of the Green Fluorescent Protein (please see the handout that accompanies the α-helix/β-sheet Collection) **Possible misconceptions to be aware of when using this kit: Amino acids are not assembled by backbone pieces first and then the addition of the sidechains. The sidechains are separate in this kit to allow for exploration of the different structures of sidechains and to allow for constructing models of the α-helix and β-sheet backbones structures. Copyright Center for BioMolecular Modeling. All rights reserved. Revised 11/12 Activities for the α-helix/β-sheet Construction Kit Page 5 of 5
Introduction 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
So 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
Secondary Structure. by hydrogen bonds
Secondary Structure In the previous protein folding activity, you created a hypothetical 15-amino acid protein and learned that basic principles of chemistry determine how each protein spontaneously folds
Lecture 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
Secondary Structure North 72nd Street, Wauwatosa, WI Phone: (414) Fax: (414) dmoleculardesigns.com
Secondary Structure In the previous protein folding activity, you created a generic or hypothetical 15-amino acid protein and learned that basic principles of chemistry determine how each protein spontaneously
CS612 - 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
Objective: 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:
Molecular 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:
PHAR3316 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
Biochemistry - 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,
Biological 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:
Amino 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
Green Segment Contents
Green Segment Contents Parts Reference Guide Green Segment 1 8 2 6 3 4 5 7 1. Amino Acid Side Chain Chart shows the properties and atomic structure of side chains. 2. Amino Acid Side Chains affect protein
Chemistry 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;
Properties 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
Biology 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
Lecture 10 More about proteins
Lecture 10 More about proteins Today we're going to extend our discussion of protein structure. This may seem far-removed from gene cloning, but it is the path to understanding the genes that we are cloning.
Introduction 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
Amino 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
CHAPTER 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)
THE 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
Proteins 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
Draw how two amino acids form the peptide bond. Draw in the space below:
Name Date Period Modeling Protein Folding Draw how two amino acids form the peptide bond. Draw in the space below: What we are doing today: The core idea in life sciences is that there is a fundamental
Copyright 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,
Biomolecules: 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
The 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
Midterm 1 Last, First
Midterm 1 BIS 105 Prof. T. Murphy April 23, 2014 There should be 6 pages in this exam. Exam instructions (1) Please write your name on the top of every page of the exam (2) Show all work for full credit
Section 1 Proteins and Proteomics
Section 1 Proteins and Proteomics Learning Objectives At the end of this assignment, you should be able to: 1. Draw the chemical structure of an amino acid and small peptide. 2. Describe the difference
The 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
1.4. 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
9/6/2011. 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
PROTEIN. By: Shamsul Azahari Zainal Badari Department of Resource Management and Consumer Studies Faculty of Human Ecology UPM
PROTEIN By: Shamsul Azahari Zainal Badari Department of Resource Management and Consumer Studies Faculty of Human Ecology UPM OBJECTIVES OF THE LECTURE By the end of this lecture, student can: Define
Mutations and Disease Mutations in the Myosin Gene
Biological Sciences Initiative HHMI Mutations and Disease Mutations in the Myosin Gene Goals Explore how mutations can lead to disease using the myosin gene as a model system. Explore how changes in the
Macromolecules 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
The 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
Amino acids. Dr. Mamoun Ahram Summer semester,
Amino acids Dr. Mamoun Ahram Summer semester, 2017-2018 Resources This lecture Campbell and Farrell s Biochemistry, Chapters 3 (pp.66-76) General structure (Chiral carbon) The amino acids that occur in
AMINO 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
Methionine (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
Chemical 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
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
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
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
Short 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
Fundamentals 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
Proteins 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
بسم هللا الرحمن الرحيم
بسم هللا الرحمن الرحيم Biochemistry Lec #1 Dr. Nafith AbuTarboush- (30.6.2014) Amino Acids 1 Campbell and Farrell s Biochemistry, Chapter 3 (pp.66-76) Introduction: Biochemistry is two courses; one is
Page 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
Gentilucci, 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
Q1: 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
Amino acids. You are required to know and identify the 20 amino acids : their names, 3 letter abbreviations and their structures.
Amino acids You are required to know and identify the 20 amino acids : their names, 3 letter abbreviations and their structures. If you wanna make any classification in the world, you have to find what
Raghad 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:
Moorpark 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
Fatty acids and phospholipids
PYS 4xx Intro 2 1 PYS 4xx Intro 2 - Molecular building blocks We now describe in more detail the nomenclature and composition of several classes of compounds of relevance to the cell, including: membrane
AP 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,
Reactions 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
Human 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
Protein Folding LARP
Protein Folding LARP Version: 1.0 Release: April 2018 Amplyus 2018 minipcr TM Protein Folding LARP (Live Action Role Play) Summary Materials In this activity, students will role play to make a folded protein
Amino Acids. Amino Acids. Fundamentals. While their name implies that amino acids are compounds that contain an NH. 3 and CO NH 3
Fundamentals While their name implies that amino acids are compounds that contain an 2 group and a 2 group, these groups are actually present as 3 and 2 respectively. They are classified as α, β, γ, etc..
I) 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
Different 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
Chapter 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,
AMINO ACIDS NON-ESSENTIAL ESSENTIAL
Edith Frederika Introduction A major component of food is PROTEIN The protein ingested as part of our diet are not the same protein required by the body Only 40 to 50 gr of protein is required by a normal
1. Describe the relationship of dietary protein and the health of major body systems.
Food Explorations Lab I: The Building Blocks STUDENT LAB INVESTIGATIONS Name: Lab Overview In this investigation, you will be constructing animal and plant proteins using beads to represent the amino acids.
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,
PROTEINS. 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
Lipids: 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
Practice 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
CHEM-342 Introduction to Biochemistry Your Name Final Examination - Individual (Part I) Friday, 26 May :30 12:15 PM H. B. White - Instructor
HEM-342 Introduction to Biochemistry Final Examination - Individual (Part I) Friday, 26 May 2006 10:30 12:15 PM H. B. White - Instructor Range 28-72(2) out of 85, Average 53.5 Important - Please read this
Review 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
BIO 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
Amino 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
COO - 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
Chapter 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
Biochemistry 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)
Macromolecules 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
Distribution of the amino acids in Nature Frequency in proteins (%)
Distribution of the amino acids in ature Amino Acid Frequency in proteins (%) Leucine Alanine Glycine erine Valine Glutamic acid Threonine Arginine Lysine Aspartic acid Isoleucine Proline Asparagine Glutamine
Structure 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
Towards a New Paradigm in Scientific Notation Patterns of Periodicity among Proteinogenic Amino Acids [Abridged Version]
![Towards a New Paradigm in Scientific Notation Patterns of Periodicity among Proteinogenic Amino Acids [Abridged Version]](/thumbs/84/90818314.jpg "Towards a New Paradigm in Scientific Notation Patterns of Periodicity among Proteinogenic Amino Acids [Abridged Version]")
Earth/matriX: SCIENCE TODAY Towards a New Paradigm in Scientific Notation Patterns of Periodicity among Proteinogenic Amino Acids [Abridged Version] By Charles William Johnson Earth/matriX Editions P.O.
PROTEINS. 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,
Maha 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
M1 - Renal, Fall 2007
University of Michigan Deep Blue deepblue.lib.umich.edu 2007-09 M1 - Renal, Fall 2007 Lyons, R.; Burney, R. Lyons, R., Burney, R. (2008, August 07). Renal. Retrieved from Open.Michigan - Educational Resources
Amino acids. Dr. Mamoun Ahram and Dr. Diala Abu-Hassan Summer semester,
Amino acids Dr. Mamoun Ahram and Dr. Diala Abu-Hassan Summer semester, 2017-2018 dr.abuhassand@gmail.com Resources This lecture Campbell and Farrell s Biochemistry, Chapters 3 (pp.66-76) General structure
Insulin mrna to Protein Kit
Insulin mrna to Protein Kit A 3DMD Paper BioInformatics and Mini-Toober Folding Activity Student Handout www.3dmoleculardesigns.com Insulin mrna to Protein Kit Contents Becoming Familiar with the Data...
Biomolecule Stations
AP Biology Biomolecule Stations Names Per. In this two-day activity, you will move through several different stations and learn about the four macromolecules in the biological world. Day 1: Modeling Carbohydrates
Guided Inquiry Skills Lab. Additional Lab 1 Making Models of Macromolecules. Problem. Introduction. Skills Focus. Materials.
Additional Lab 1 Making Models of Macromolecules Guided Inquiry Skills Lab Problem How do monomers join together to form polymers? Introduction A small number of elements make up most of the mass of your
Moorpark College Chemistry 11 Fall Instructor: Professor Gopal. Examination #5: Section Five December 7, Name: (print) Section:
Moorpark College Chemistry 11 Fall 2011 Instructor: Professor Gopal Examination #5: Section Five December 7, 2011 Name: (print) Section: alkene < alkyne < amine < alcohol < ketone < aldehyde < amide
Introduction 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.
1. (38 pts.) 2. (25 pts.) 3. (15 pts.) 4. (12 pts.) 5. (10 pts.) Bonus (12 pts.) TOTAL (100 points)
Moorpark College Chemistry 11 Spring 2010 Instructor: Professor Torres Examination #5: Section Five May 4, 2010 ame: (print) ame: (sign) Directions: Make sure your examination contains TWELVE total pages
Judy Wieber. Department of Computational Biology. May 27, 2008
Review II: The Molecules of Life Judy Wieber BBSI @ Pitt 2008 Department of Computational Biology University it of Pittsburgh School of Medicine i May 27, 2008 Outline Introduction Proteins Carbohydrates
استاذ 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
This exam consists of two parts. Part I is multiple choice. Each of these 25 questions is worth 2 points.
MBB 407/511 Molecular Biology and Biochemistry First Examination - October 1, 2002 Name Social Security Number This exam consists of two parts. Part I is multiple choice. Each of these 25 questions is
Biomolecule Stations
AP Biology Biomolecule Stations Names Per. In this two-day activity, you will move through several different stations and learn about the four macromolecules in the biological world. Day 1: Modeling Carbohydrates
a) 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
Biology. 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,
Introduction. Basic Structural Principles PDB
BCHS 6229 Protein Structure and Function Lecture 1 (October 11, 2011) Introduction Basic Structural Principles PDB 1 Overview Main Goals: Carry out a rapid review of the essentials of protein structure
Organic 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
For 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
Protein Structure Klemens Wild, BZH,
Protein Structure recommended books Proteins protein definition From gr. proteios (superior, erstrangig) 1836 JJ Berzelius Functions: structural, enzymes, muscle, transport immune system, Linear polymer
Lecture 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