Answers_to_protein_study_guide

Answers_to_protein_study_guide - Answers to study guide 3...

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Answers to study guide 3 (Kopachik) 1. Why are protein polymers so versatile in numbers of proteins and in ability to interact with other molecules in the cell and so cause physiological changes to occur? Proteins can be made to be different in the number of amino acids and the sequence of amino acids. Because there are 20 choices for amino acids at each monomer addition site there is a fantastic number of possibilities. For instance 20 360 is the number of variations of an average sized protein. This very high number of sequences for polypeptides means that a fantastically large number of different shapes and surfaces are possible for these macromolecules. The proteins in cells are a selected set of these that have very specific roles to play in interacting with other molecules in the cell. 2. Draw a generic amino acid and describe the main functional groups? Use the terms alpha carbon, amino group, carboxylic acid group, R group. H | NH 2 - C - COOH | R Amino group ionized to NH 3 + and carboxyl group ionized to COO - at pH 7. R side group is any one of just 20 possible groups: they play roles in determining the shape and therefore function of the protein. R groups can be uncharged, acidic, basic or hydrophilic or hydrophobic. Classification of the R groups: 1. hydrophilic: with hydroxyl, sulfhydryl, carboxylic groups generally on the outside of proteins. 2. hydrophobic: with nonpolar R groups internal location. - the R groups determine solubility, shape, and therefore function 3. From Fig. 5.17 be able to recognize amino acids that would be nonpolar, polar or electrically charged. You do not have memorize the R groups but instead be able to
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This note was uploaded on 02/03/2012 for the course BS 111 taught by Professor Patterson during the Spring '05 term at Michigan State University.

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Answers_to_protein_study_guide - Answers to study guide 3...

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