Chapter 4 Flashcards
α helix only
- Cylinder Structure
2. One full turn every 3.6 amino acids
β sheet only
- Consists of antiparallel or parallel strands
2. Side Chains alternating above and below the structure
Both α helix & β sheet
- Can be formed by many sequences
2. Formed by hydrogen-bonding between backbone atoms
The antibody is composed by __ polypeptide chains
4
If SDS-PAGE were used for a pure sample of this protein that was preincubated with mercaptoethanol, then there would be __ bands expected.
2
How do most motor proteins ensure their movements are unidirectional?
They couple a conformational change to the hydrolysis of an ATP molecule.
A disulfide bond is a ___ interaction within the protein.
covalent
Protein molecules that have a quaternary structure must have two or more of which of the following?
polypeptide chains
What is the definition of a protein-binding site?
any region on a protein’s surface that interacts with another molecule through “noncovalent” bonding.
What are protein families?
Evolutionary related proteins that are similar in amino acid sequence and three-dimensional conformation.
In a globular protein, where would the amino acid tryptophan most likely be found?
buried in the protein’s interior
What does the primary structure of a protein refer to?
The linear amino acid sequence of the protein.
What do the segments of a transmembrane protein that cross the lipid bilayer usually consist of?
an α helix with mostly nonpolar side chains
For which reason are α helices and β sheets common folding patterns in polypeptides?
The amino acid side chains are not directly involved in their formation.
The protein can be unfolded by a process called ____
Denaturation
Generally speaking, what determines the biological activity of a protein?
amino acid sequence.
What provides the information necessary to specify the three-dimensional shape of a protein? Choose the best answer in the context of which generally applies to most proteins.
protein’s amino acid sequence.
Which part of an amino acid gives it its unique properties?
side chain.
Which part of amino acids are involved in a peptide bond?
amino group of one amino acid and carboxyl group of the other.
Hydrogen bonding between N-H and C=O groups of every fourth amino acid within a polypeptide chain results in which type of folding pattern?
a helix
A stretch of amino acids in a polypeptide chain that is capable of independently folding into a defined sturcture is called a ____
domain
A binding site on the surface of a protein interacts specifically with another protein through___
many weak noncovalent interactions.
How does phosphorylation of a protein affect its activity?
It could increase or decrease activity.
How many amino acids are commonly used in making proteins?
20