MCDB 310 Study Guide - Midterm Guide: Circular Dichroism, Ramachandran Plot, Beta Sheet

93 views13 pages

blushprairie-dog461

10 Oct 2018

School

U of M

Department

Molec, Cell & Develop Biology

Course

MCDB 310

Professor

Kenneth Balazovich

For unlimited access to Study Guides, a Grade+ subscription is required.

Document Summary

Be able to connect two amino acids with a peptide bond. Bond between c-n, loss of water (oh from carbonyl and h from amino groups) Large dipole moment in trans configuration due to partial + and partial - charges on the n and o. The peptide bond is planar due to resonance. The bonds between the n-calpha and calpha-c can rotate (single bonds with phi/psi angles) Given the structure of a peptide backbone, be able to indicate the phi and psi angles. Phi is between n-c and psi is between c-c. Be able to briefly describe what a ramachandran plot is and why we use them. Ramachandran plots show combinations of psi and phi angles for a protein that are either favorable or unfavorable. The white space represents unfavorable combinations then the colored spaces represent favorable and can also predict the secondary structure. When several peptides in a row adopt similar phi/psi combinations, this gives rise to secondary structures.

Related Questions

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

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.

maroonwallaby335

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

violetyellowjacket662

Each of the following can cause a protein to denature except:

Select one:

a. enzyme treatment

b. heat

c. change in pH

d. detergents

What factors can influence the speed of a reaction by an enzyme?

Select one:

a. The weakening of bond energies in the reactants

b. The closeness of the reactants to each other in the active site

c. The orientation of the reactants

d. All of these

A protein that is comprised of two or more protein chains that interact to make the overall structure is called the:

Select one:

a. quaternary structure

b. secondary structure

c. primary structure

d. tertiary structure

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

Select one:

a. Dipole-dipole

b. Hydrogen bonding between the carbonyl group and amino group

c. Salt bridges

d. Peptide bonds

A molecule that is similar in terms of the correct structure to the substrate for an enzyme will probably be a:

Select one:

a. competitive inhibitor

b. regulator

c. cofactor

d. noncompetitive inhibitor

sapphireraccoon216

MCDB 310 Study Guide - Midterm Guide: Circular Dichroism, Ramachandran Plot, Beta Sheet

Document Summary

Get access

Related Documents

MCDB 310 Study Guide - Midterm Guide: Van Der Waals Radius, Covalent Bond, Asymmetric Carbon

MCDB 310 Midterm: Biochemistry Exam 1 Review

MCDB 310 Study Guide - Midterm Guide: Gibbs Free Energy, Ribosome Biogenesis, Weak Interaction

Related Questions