BIOCHEM 2EE3 Lecture Notes - Lecture 3: Thioether, Arginine, Asparagine

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blackherring683

7 Mar 2018

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L is the only form that occurs in cells glycine is the only amino acid that is achiral. Aliphatic - non polar and hydrophobic placed in the order gavli - hydrophobicity of amino acid increases with increasing number of carbon atoms in side chain. Aa prefer to reside inside protein molecule glycine and alanine are exception - they are ambivalent and can reside anywhere on protein bc side chains are small. Gly (g), ala (a), val (v), leu (l), ile (i) Cyclic - proline has secondary amino group its side chain forms covalent bond with amino group aliphatic, but found frequently on surface of proteins bc of rigid ring structure suited for u- turns in protein structures. Aromatic - hydrophobic and aromatic absorb uv light at wavelength ~280nm can use this feature to measure protein concentrations given that proteins measured contain these aromatic amino acids. Y has ionizable group although y and w both have some polar character.

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b) SELECT TWO

Select all the following that can be used to describe the sturcture of enzymes, the importance of the shape, and the relationship of enzyme shape and function.

Check all that apply.

1. Amino acids are linked by hydrogen bonds with various chemical groups attached to give enxymes their two dimensional shape.

2. Amino acids are linked by hydrogen bonds with various chemical groups attached to give enxymes their three dimensional shape.

3. Amino acids are linked by hydrogen bonds with various chemical groups attached to give enzymes their four dimensional shape.

4. Aminso acids are linked by peptide bonds with hydrogen bonds between nearby amino and carboxyl groups to give enzymes their two dimensional shape.

5. Amino acids are linked by peptide bonds with various chemical groups attached to give enzymes their four dimensional shape.

6. one or more polypeptide chains are folded and bond together in the fourth level of protein organization.

7. The shape of an enzyme determnes its function.

8. The number of amino acids in an enzyme determines its function.

9. The active sit binds with the substrate.

10. enzymes are substrate specific.

11. Alteration of active sites does not alter the enzymatic reaction.

For each of the following sentences, fill in the blanks with the best word or phrase selected from the list below. Not all words or phrases will be used; each word or phrase should be used only once. Proteins are ______________ built from amino acids, which each have an amino group and a _____________ group attached to the central _______________. There are twenty possible _______________ that differ in structure and are generally referred to as âR.â In solutions of neutral pH, amino acids are _______________, carrying both a positive and negative charge. When a protein is made, amino acids are linked together through _______________, which are formed by condensation reactions between the carboxyl end of the last amino acid and the ___________________ end of the next amino acid to be added to the growing chain.

a: amino	b: ionized	c: polypeptides
d: alpha-carbon	e: length	f: protein
g: carbon	h: noncovalent	i: R group
j: carboxyl	k: peptide bonds	l: side chains

m: hydroxide

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BIOCHEM 2EE3 Lecture Notes - Lecture 3: Thioether, Arginine, Asparagine

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