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BIOCHEM 2EE3 Lecture Notes - Lecture 4: Coiled Coil, Alpha Helix, 310 Helix

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indigohornet100
3 Apr 2018
School
McMaster University
Department
Biochemistry
Course
BIOCHEM 2EE3
Professor
Russell Bishop

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Document Summary

Function of a protein is dictated by it"s structure and the structure of a protein is dictated by its primary sequence (the sequence of amino aids) Side chains have unique chemical properties which drive the folding of the protein in to a 3-d structure. Primary: the sequence of amino acids in a polypeptide chain. Secondary: starts to get into the folding bit, driven by peptide backbone interactions. The peptide bond angle is denoted by the letter omega and has a bond angle of 180 degrees (trans) An amino aid backbone has 2 freely rotated single bonds. Phi - the angle between n and c-alpha. Psi - the angle between c-alpha and carbonyl carbon. These phi, psi hinge regions have allowable movement. Steric hinderances is imposed by the peptide bond but also free rotation in p and psi bonds. Shown by ramachandran plot: is which phi, psi angles can occur in a protein (1) beta-sheets.

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Related Questions

The sequence of amino acids is considered to be the ________ structure of a protein.

Select one:

a. secondary

b. tertiary

c. quaternary

d. primary

The pattern the backbone folds, for example alpha-helix or beta pleated sheet, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

Which type of forces stabilizes the primary structure of a protein?

Select one:

a. Salt bridges

b. Hydrogen bonding between the carbonyl group and amino group

c. Dipole-dipole

d. Peptide bonds

The interaction of the side chains on the amino acids, for example hydrophobic attractions, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

thank you

1. A sequence of amino acids in a certain protein is found to be – Ser – Gly – Pro – Gly –

The sequence is most probably part of a(n):

a. beta turn

b. antiparallel beta sheet

c. alpha-helix

d. parallel beta-sheet

e. alapha-sheet

2. Which statement about peptides bonds is NOT TRUE?

There is perfectly free rotation about the peptide bond.

The peptide bond has partial double-bond character.

The peptide bond is shorter than a normal carbon-nitrogen single bond.

The peptide bond usually has a trans configuration with respect to the alpha-carbons of the two amino acids involved in the peptide bond.

Peptide bonds are made via condensation of an amine and a carboxylic acid with loss of water.

3. Which of the following statements about proteins is FALSE?

Active proteins are generally very loosely structured.

In water-soluble proteins, hydrophobic amino acid residues are generally buried and not exposed to water.

Primary structure determines tertiary structure.

Secondary structure is regular, recurring arrangements in space of nearby amino acid residues in a polypeptide.

Quaternary structure involves the interaction of subunits in a protein with more than one polypeptide chain.