Protein Structure (BIO, BC, OC)

Question 1

Primary structure of a protein

Answer 1

the linear connectivity of amino acids

Question 2

The alpha helix is stabilized by _____ bonding interactions between the _______ and _______.

Answer 2

hydrogen, peptide backbone carbonyl (C=O) oxygen atoms, peptide backbone amide groups 4 residues away

Question 3

_____ bonding is the primary stabilizing force in protein secondary structure.

Answer 3

Hydrogen

Question 4

_____ are sheetlike structures created by several regions of a peptide chain looping back along one another; these regions interact through _____ bonding interactions between ______ and ______.

Answer 4

Beta sheets, hydrogen, backbone carbonyl, amino groups

Question 5

Tertiary structure of a protein

Answer 5

the overall 3-dimensional structure that peptide chain folds into

Question 6

The peptide will fold into the most ____ favorable state that it can reach, this most ____ conformation is the peptide’s ____.

Answer 6

energetically, optimal, native state

Question 7

Internally, the peptide is stabilized by ____ bonding, ___ bonding/___ bridges, ____ interactions, _____ forces, and _____ linkages.

Answer 7

hydrogen, ionic bonding/salt bridges, dipole-dipole, London dispersion forces, disulfide linkages

Question 8

Hydrophobic interactions occur between ____ residues as they try to _____ their contact with one another and ______ their contact with water.

Answer 8

hydrophobic, maximize, minimize

Question 9

Disulfide linkages between ______ are the only _____ bond capable of influencing tertiary structure.

Answer 9

cysteines, covalent

Question 10

When a protein loses its three-dimensional shape, it’s function will be ____ or ____ unless it ____.

Answer 10

lost, altered, refolds

Question 11

Quaternary structure of a protein

Answer 11

the combination of multiple peptides together, or the combination of peptides with non-protein molecules

Question 12

When multiple peptide subunits join together, they form a ___

Answer 12

polypeptide

Question 13

Prosthetic groups are non-protein molecules which can be organic or inorganic that are ____ bound to a peptide and are ___ for protein ____.

Answer 13

tightly, required, functionality

Question 14

An _____ is a protein without its characteristic prosthetic group and are generally nonfunctional

Answer 14

apoprotein or apoenzyme

Question 15

An apoprotein that has been joined with its prosthetic groups and gained functionality is a ___

Answer 15

holoprotein

Question 16

A low energy protein is a ____ stable protein

Answer 16

more

Question 17

In an aqueous environment, ____ residues will want to be positioned on the outside of a protein

Answer 17

hydrophilic

Question 18

at a high pH, more of the proteins residues will be ____

Answer 18

deprotonated

Question 19

at high salinity, internal ____ interactions within the protein will be disrupted, impeding folding.

Answer 19

ionic