BIS 102 Lecture Notes - Lecture 7: Protein Structure, Hydrogen Bond, Protein Folding

11 views2 pages

viridianwallaby406

3 Apr 2021

School

Department

Course

Professor

For unlimited access to Class Notes, a Class+ subscription is required.

Document Summary

Different levels of protein structure to primary structure : covalent bonds. C - terminus polypeptide backbone o_0-0-0-0-0 - l l. " regular. repeating pattern among contiguous aa residues. " reverse tum ( b - bend) : not repeating , only 1 hydrogen bond. " hydrophobic effect t 3 other weak bonds t - s - s - 40 quaternary structure : multiple polypeptides / subunits. Hydrophobic effect t 3 other weak bonds t - s - s - to primary structure. A - h - p - v - v - v - h - k amino acid sequence. 10 structure determines 30 structure ( information protein folding biological function) 30 the most thermodynamically stable due to tweak bonds. Spontaneously folds into 30 structure , no energy input. Used to determine relation to other proteins. Experiment with an9109em in 117000 mw) it ang 109m in times. ""fifer incubate i s r embryo chicken egg new blood vessels !

Related Questions

1. The level of protein structure that is stabilized primarilyby non-covalent interactions between the side chains within asingle polypeptide chain is refered to as its:

A) primary structure

B) secondary structure

C) tertiary structure

D) quaternary structure

E) none of the above

2. Collagen, a strong fibrous protein found in connectivetissue, bone, and the extracellular matrix, has a structure inwhich three left-handed helices wind around each other to form aright-handed triple helix. The primary structure of collagen has arepeat unit of -(Gly-X-Pro)- Which of the following bonds stabilizethe collagen triple helix? (mark all that apply)

A) Hydrogen bonds between hydroxyproline residues

B) Hydrogen bonds between N-H and C=O

C) Ionic bonds between amino acid side chains

D) Hydrogen bonds between charged amino acids

3. The non-covalent forces that stabilize the Beta-strandconformation of peptides include:

A) H-bonds between amide C=O and amide NH

B) Van der Waals packing between the peptide backbone atoms

C) Van der Waals packing due to side chain interdigitation

D) Only A and B above

E) None of the above

4. What is the approximate length difference of a 22-kDasingle-stranded ?-helical protein segment vs. a 22-kDasingle-stranded ?-strand protein segment? Assume a mean residuemass of 110 Da. Show work.

5. Circular dichroism measurements have shown that the peptidebackbone of poly-l-lysine (KKKKKKK) adopts a random coilconformation at pH 7.0, but becomes ?-helical as the pH is raisedabove 10. This observation is known as the

magentaotter572

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

Please I need help with these questions

1. The word "quaternary" structure refers to which case of "4"?

a)the 4^th residue in the sequence just those proteins with 4 total subunits, such as hemoglobin

b)proteins with any number of multiple subunits, regardless of the total number (2, 3, 4, 5, ...)

c) the number of residues per turn in an alpha helix (3.6 rounded off to the closest integer, which is 4)

d)the number of residues (4 total) needed to make a beta turn

2. The Ramachandran plot depicts which of the following?

a.sterically permitted rotational (dihedral) angles along the backbone chain

b.the polar and nonpolar sides of helices, using circular graph paper

c.the cysteine pairing pattern in a protein having several disulfide bonds

3. The "level" of protein structure involving repetition of a particular choice of phi and psi angles is which of the following?

a. primary structure

b. secondary structure

c. tertiary structure

d. quaternary structure

BIS 102 Lecture Notes - Lecture 7: Protein Structure, Hydrogen Bond, Protein Folding

Document Summary

Get access

Related Documents

BIS 102 Lecture Notes - Lecture 2: Home Shopping Network, Globular Protein, Acid Dissociation Constant

Related Questions