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Biochem Exam 2 HW Questions
Terms in this set (24)
A phylogenetic tree depicts ___________ of proteins.
Identify the least conservative amino acid substitution, assuming that these two residues occur at the same position in two homologous proteins.
Identify the most conservative amino acid substitution, assuming that these two residues occur at the same position in two homologous proteins.
Paralogous genes are
The Results of Gene Duplication
Noncovalent forces that stabilize protein structure include all of the following except
Which one of the following sequences of five amino acids would most likely be located in the interior of a water soluble globular protein?
What ultimately determines the unique three dimensional structure of soluble globular proteins?
The Sequence Of The Amino Acid Residues
Which of the following sequences of amino acids is most likely to be at the surface of a water-soluble globular protein?
You have been shown the detailed 3-D structure of an unknown protein. The information indicates that the protein's non-polar amino acid side chains are all exposed on the surface, whereas its polar side chains are all "buried" in the interior. What can you conclude about this protein?
Intergral Membrane Protein
Which treatment is least likely to cause a protein to denature?
High Concentration Of Salts
What is the probability of refolding a denatured protein to its native conformation, in which three disulfide bonds can form randomly from 6 Cys residues?
Which of the following amino acids combinations have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein?
Glu and Lys
The low pH found in the gut can enhance the digestibility of dietary protein by causing
If hydrogen bonding were the most important feature in determining strength in fibrous proteins, which of the following sequences likely has the highest melting temperature and why
"1" because Hyp has OH groups
Which of the following occurs first when folding a disordered polypeptide chain into a stable protein formation?
Aggregation Of Hydrophobic Regions In The Protein
In general molecular chaperone proteins function by
Preventing Premature Folding By Binding Hydrophobic Regions Of The Protein.
Proteins form identical disulfide bonds both in vitro and in vivo.
Chaperonins such as the GroEL/ES system
Require ATP Hydrolysis
Where are irregular secondary structures (loops) generally found in soluble globular proteins and why?
On The Surface So That They Can Interact With The Solvent
Which statement below does not describe fibrous proteins?
Domains Have A Globular Fold
Bioinformatics can help you predict only your secondary structure, but not tertiary or quaternary.
Globular proteins are found mainly in the
Domains that have more than 40% identical sequence usually have the same function
Fibrous proteins have a repetitive structure
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