Protein structure question..?

Question

There is 4 structures ... quaternary, teritary, secondary, and primary..however I am having a hard time matching these descriptions to each of them.

A. Overall 3 dimensional shape
B. Amino acid sequence
C. Even a slight change in this can alter Tertiary structure
D. This level occurs in proteins with more than one polypeptide subunit
E. Coling and folding produced by hydrogen bonds between --NH and C=O groups
F. Not present in all proteins
G. Level of structure that is held together by peptide bonds
H. Alpha helix and pleated sheet
I. Stabilized by clustering of hydrophobic R groups, hydrogen bonds, ionic bonds, and sometimes even covalent bonds
J. "Globular" or "fibrous" might describe this level of structure

I am supposed to match each one of these to one of the 4 structures of the protein.

Answer 1

Primary: B, G

Secondary: C, E, H

Tertiary: J, I (although I thought there were NO covalent bonds here, but maybe its just MOSTLY noncovalent bonds...)

Quaternary: A, D, F,



Hope that helps!

Answer 2

Primary: B, C, G

Secondary: E, H

Tertiary: A, J, I

Quaternary: D, F

Answer 3

a million. secondary shape is the uncomplicated repeating 3 dimensional instruments interior the protein (as detrimental to regular shape that's basically the sequence of the amino acids), maximum in many situations alpha helix or beta pleated sheet. 2. peptide communities (peptide bonds) carry the amino acids at the same time interior the chain or backbone of the protein, yet they are additionally in contact in hydrogen bonding between amino acids at a distance from one yet another, which ends interior the contorsion of the chain which leads to e.g. and alpha helix 3. returned, a mixture of hydrogen bonding interior the secondary shape and the hydrophobicity of the realm chains on the exterior reasons the secondary shape to fold