Protein structure

1 Kingston College Biology CAPE Unit 1 Proteins Worksheet Name: ________________________________ Date: _________________________ 1. Draw a simple amino acid molecule and label each part. [3] 2. Polypeptide chains are formed by ______________ bonding and is added to the _________________________ of amino acid. Use a diagram to show a dipeptide below [4] (make sure you label the bond mentioned above) 3. What type of bonding is responsible for the primary structure of proteins and what is the primary structure? [2] ___________________________________________________________________________________________ ___________________________________________________________________________________________

proteins

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Biology

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Biology

Protein

Peptide

health

1 LECTURE 6: PROTEINS Protein Outline 2 Proteins (structure and function) ?Major roles in physiology & structural frameworks ?Amino acid structure ?Levels of structural organization: (primary, secondary, tertiary, quaternary) ?Properties (relate to structure) ? Major classes of proteins Objectives 3 1. Describe the structure of amino acids 2. Outline how proteins are formed by peptide bonds. 3. Describe how proteins are organized at the primary, secondary, tertiary, quaternary levels. 4. State the functions of proteins 5. Classify proteins according to structure/solubility, composition, function. Proteins 4 ?More than 50% of the dry mass of an organism consists of proteins.

Bio_160_Lecture1

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Biology

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Chemistry

Functional Groups

Organic compounds

Acids

Equilibrium chemistry

Monomer

Biology 160 Lecture 1 Introduction, Chemistry and Molecules Introductory Concepts for Studying Biology & Science ? Chapter 1 What is science? ? Knowledge gained through careful observation, experimentation and reasoning. ? Science is: ? Explanatory ? Testable ? Reproducible ? Predictive ? Tentative Questions of Science Scientific discoveries create complex questions: ? Ex. Atom ? Should scientists be free to pursue any research? ? Cloning/Stem cell. ? Should government control scientific progress? ? Progression of science. ? Research normally follows a logical progression. ? Interest focuses on problems that impact humanity. The Importance of Publication ? Results of research are submitted for publication. ? peer review by other

2002 nobel prize information: bio

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Biology

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Chemistry

Laboratory techniques

Science

Matrix-assisted laser desorption/ionization

Soft laser desorption

Nuclear magnetic resonance

BIology Nobel Prize Abstract

10/1/13 The 2002 Nobel Prize in Chemistry - Popular Information www.nobelprize.org/nobel_prizes/chemistry/laureates/2002/popular.html 1/10 The Nobel Prize in Chemistry 2002 John B. Fenn, Koichi Tanaka, Kurt W?thrich ( nglish Swedish Popular Information Information for tK H PuEliF 9 October 2002 The Nobel Prize in Chemistry for 2002 is being shared between scientists in two important fields: mass spectrometry (MS) and nuclear magnetic resonance (NMR). The Laureates, John B. Fenn and Koichi Tanaka (for MS) and Kurt W?thrich (for NMR), have contributed in different ways to the further development of these methods to embrace biological macromolecules. This has meant a revolutionary breakthrough, making

AP Biology Macromolecules

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Biology

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Biology

Protein

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Macromolecules Macromolecules The topic of macromolecules lends itself well to illustrate three integral themes woven throughout the text and course: There is a natural hierarchy of structural level in biological organization As one moves up the hierarchy, new properties emerge because of interactions among subunits at the lower levels Form fits function. Most macromolecules are polymers Polymer = (Poly = many; mer = part) Large molecule consisting of many identical or similar subunits connected together. Monomer = Subunit or building block molecule of a polymer. Macromolecule = (Macro large) Large organic polymer. Formation of macromolecules from smaller building block molecules represents another level in the hierarchy of biological organization.