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