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Biochem Test 1
Terms in this set (27)
What are the key properties of proteins?
a. Proteins are linear polymers composed of amino acids Correct
b. Proteins have a wide variety of functional groups Correct
c. Proteins can interact with one another and other macromolecules to form complexes Correct
d. Proteins need to be both flexible and rigid
Which of the following amino acids has an uncharged side chain under physiological conditions
Why do humans only have ~25,000 protein encoding genes?
a. Some proteins are inherently unstructured and can exist in multiple conformations Correct
b. Meaning that the same set of genes can encode for intrinsically unstructured proteins Correct
c. that do not have defined structure under physiological conditions until the interact with other molecules Correct
d. example lymphotactin exist in two conformations at equilibrium both do a unique job and are required to carry out a specific function
The process of protein folding involves:
progressive stabilization of correct secondary structural intermediates, and unfolding of incorrect structures, until the final structure is attained.
What would happen to your cumulatively selected conformations if a more energetically favored structure came along?
a. One result could be the manifestation of amyloid diseases Correct
b. An amyloid is an extracellular, proteinaceous deposit exhibiting beta sheet structure Correct
c. The subtle change creates an aggregate that increases entropy and thus the free energy Correct
d. One example of this are infectious prions versus normal prions
What is the only isomer configuration in biological systems?
Which of the following statements regarding peptide bonds is least accurate
Favored conformation of peptide bonds is with the sequential alpha carbons in the cis position.
At what pH does the 'backbone' structure of all amino acids form a zwitter ion?
Which of the following best describes an alpha-helical region of a polypeptide?
Right-handed, 3.6 aa/turn
Which of the following best describes the arrangement of amino acid side chains in an alpha helix?
The side chains point outward away from the helical axis.
What group of amino acids does histidine belong to?
Which of the following amino acids is found most frequently at beta turns in the secondary structures of proteins
What chemical properties keep the polypeptide residue in a planar formation?
a. resonance; which influences molecular geometry
b. The trans conformation
d. limited amount of torsion angles
Which of the following secondary structures is most likely to be found in a membrane-embedded portion of a protein?
An alpha helix composed entirely of hydrophobic residues
The _____________ structure is formed by hydrogen bonds between peptide NH and CO groups of amino acids that are near one another in the primary structure
Which protein secondary structure is stabilized primarily by intrachain hydrogen bonds
What secondary structure is formed by adjacent Beta-strands?
Which of the following determines a protein's native structure?
The protein's linear amino acid sequence
How do primary polypeptides fold to native proteins in seconds rather than years?
a. cumulative selection
b. thermodynamically more favorable structures are retained
c. Progressive stabilization of secondary (local) structure
d. Chaperone proteins
The molecular interaction called "hydrophobic effect" is best described as:
The tendency of non-polar molecules to avoid interactions with water and thus aggregate.
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