BIOCHEM 4511: Dr. Wu: CH. 5-6 Mastering
exam 2024 midterm
In considering protein secondary structure which of the following is
INCORRECT? - ANSWER-The 310 helix is right-handed and often
contains proline residues
The amino acid side chain residues in an α helix point ________ away
from the center of the helix. - ANSWER-Outward
__________ between amide protons and carbonyl oxygens is necessary
to stabilize a regular folding of protein secondary structure. - ANSWER-
Hydrogen Bonding
A ________ plot describes which structures in a polypeptide are
sterically possible and which are not based on the angles of rotation
about the backbone Namide -Cα and Cα-Ccarbonyl bonds. - ANSWER-
Ramachandran
Proteins have an asymmetrical tertiary structure, while multi-subunit
proteins can exhibit several types of symmetry. - ANSWER-True
, The functional organization of proteins where specific complexes of two
or more polypeptides are formed is called ________ structure. -
ANSWER-Quaternary structure
To what level of structure do α-helices belong? - ANSWER-Secondary
structure
What is TRUE about the rotation of bonds in a protein backbone? -
ANSWER-The bond between the carbonyl carbon and nitrogen is
restricted. Other bonds are free to rotate depending only on steric
hindrance or the presence of proline residues.
The conformation of the backbone of a polypeptide is described
completely by the angle(s) of rotation about which bond(s)? - ANSWER-
N-Cα and Cα-C bonds only
Ramachandran determined the "allowed" values of the phi and psi
angles primarily by considering ________. - ANSWER-Steric Hindrance
The amino acid that destabilizes alpha-helical structures and is usually
found at the ends of alpha helices is______________. - ANSWER-
Glycine
Proline is NOT often found in α-helices of proteins because it - ANSWER-
Lacks a hydrogen atom on its amide nitrogen
exam 2024 midterm
In considering protein secondary structure which of the following is
INCORRECT? - ANSWER-The 310 helix is right-handed and often
contains proline residues
The amino acid side chain residues in an α helix point ________ away
from the center of the helix. - ANSWER-Outward
__________ between amide protons and carbonyl oxygens is necessary
to stabilize a regular folding of protein secondary structure. - ANSWER-
Hydrogen Bonding
A ________ plot describes which structures in a polypeptide are
sterically possible and which are not based on the angles of rotation
about the backbone Namide -Cα and Cα-Ccarbonyl bonds. - ANSWER-
Ramachandran
Proteins have an asymmetrical tertiary structure, while multi-subunit
proteins can exhibit several types of symmetry. - ANSWER-True
, The functional organization of proteins where specific complexes of two
or more polypeptides are formed is called ________ structure. -
ANSWER-Quaternary structure
To what level of structure do α-helices belong? - ANSWER-Secondary
structure
What is TRUE about the rotation of bonds in a protein backbone? -
ANSWER-The bond between the carbonyl carbon and nitrogen is
restricted. Other bonds are free to rotate depending only on steric
hindrance or the presence of proline residues.
The conformation of the backbone of a polypeptide is described
completely by the angle(s) of rotation about which bond(s)? - ANSWER-
N-Cα and Cα-C bonds only
Ramachandran determined the "allowed" values of the phi and psi
angles primarily by considering ________. - ANSWER-Steric Hindrance
The amino acid that destabilizes alpha-helical structures and is usually
found at the ends of alpha helices is______________. - ANSWER-
Glycine
Proline is NOT often found in α-helices of proteins because it - ANSWER-
Lacks a hydrogen atom on its amide nitrogen
