Exam 1 Cell Biology (BIOL 4100) Seibenhener Questions
With Complete Solutions
_______________________________ is the most common type
of protein-protein contact? Correct Answers Surface:Surface
2 other examples of heat shock proteins Correct Answers
HSP90 and HSP100
Affinity Correct Answers Binding ability of the enzyme to the
substrate
Alpha Helix Correct Answers slinky shape
Most common secondary structural element
Allows for compaction
Good for interactions with environment
amino terminus (N-terminus) Correct Answers start of a
protein or polypeptide referring to the free amine group (-NH2)
located at the end of a polypeptide
Beta sheets
Difference between alpha helix and beta sheets?
Antiparallel?
Parallel? Correct Answers two or more strands widely
separated in the primary sequence orient side-by-side with
hydrogen bonds between the strands
,Unlike the α helix, the ß sheet is formed by hydrogen bonds
between protein strands, rather than within a strand.
Side-by-side connected with hydrogen bonds; Antiparallel ß
sheets are slightly more stable than parallel ß sheets because the
hydrogen bonding pattern is more optimal.
Beta sheets are parallel if the polypeptide strands run in the
same direction, N-terminus to C-terminus. The N-terminus of
one beta strand will be opposite the N-terminus of the other beta
strand.
The parallel arrangement is less stable because the geometry of
the individual amino acid molecules forces the hydrogen bonds
to occur at an angle, making them longer and thus weaker
Beta turn
How many residues?
The polypeptide chain is forced to reverse direction making
______________________ possible?
Which residue is always in a beta turn? Why? Correct Answers
Simplest secondary structure
3 or 4
makes compact folding possible
Always has glycine because the R group of glycine is just a
hydrogen --> no turn restriction, allows for the 180 hairpin turn
, Binding site Correct Answers the region of a protein that
associates with a ligand; usually consists of a cavity in the
protein surface formed by a particular arrangement of amino
acid side chains
Carbohydrates:
Basic unit = ?
Atoms = ?
Function = ? Correct Answers Basic unit = sugar
Atoms = CHO
Provides energy and structural support to the cell
carboxyl terminus (c-terminus) Correct Answers the end of an
amino acid chain (protein or polypeptide), terminated by a free
carboxyl group (-COOH)
Chaperones
What proteins do chaperones normally interact with?
What proteins do chaperones not interact with?
What process do they require?
Why are they necessary? Correct Answers bind to partly
folded polypeptide chains and help them progress along the
most energetically favorable folding pathway
Interacts with unfolded, misfolded, or partially folded
polypeptides
With Complete Solutions
_______________________________ is the most common type
of protein-protein contact? Correct Answers Surface:Surface
2 other examples of heat shock proteins Correct Answers
HSP90 and HSP100
Affinity Correct Answers Binding ability of the enzyme to the
substrate
Alpha Helix Correct Answers slinky shape
Most common secondary structural element
Allows for compaction
Good for interactions with environment
amino terminus (N-terminus) Correct Answers start of a
protein or polypeptide referring to the free amine group (-NH2)
located at the end of a polypeptide
Beta sheets
Difference between alpha helix and beta sheets?
Antiparallel?
Parallel? Correct Answers two or more strands widely
separated in the primary sequence orient side-by-side with
hydrogen bonds between the strands
,Unlike the α helix, the ß sheet is formed by hydrogen bonds
between protein strands, rather than within a strand.
Side-by-side connected with hydrogen bonds; Antiparallel ß
sheets are slightly more stable than parallel ß sheets because the
hydrogen bonding pattern is more optimal.
Beta sheets are parallel if the polypeptide strands run in the
same direction, N-terminus to C-terminus. The N-terminus of
one beta strand will be opposite the N-terminus of the other beta
strand.
The parallel arrangement is less stable because the geometry of
the individual amino acid molecules forces the hydrogen bonds
to occur at an angle, making them longer and thus weaker
Beta turn
How many residues?
The polypeptide chain is forced to reverse direction making
______________________ possible?
Which residue is always in a beta turn? Why? Correct Answers
Simplest secondary structure
3 or 4
makes compact folding possible
Always has glycine because the R group of glycine is just a
hydrogen --> no turn restriction, allows for the 180 hairpin turn
, Binding site Correct Answers the region of a protein that
associates with a ligand; usually consists of a cavity in the
protein surface formed by a particular arrangement of amino
acid side chains
Carbohydrates:
Basic unit = ?
Atoms = ?
Function = ? Correct Answers Basic unit = sugar
Atoms = CHO
Provides energy and structural support to the cell
carboxyl terminus (c-terminus) Correct Answers the end of an
amino acid chain (protein or polypeptide), terminated by a free
carboxyl group (-COOH)
Chaperones
What proteins do chaperones normally interact with?
What proteins do chaperones not interact with?
What process do they require?
Why are they necessary? Correct Answers bind to partly
folded polypeptide chains and help them progress along the
most energetically favorable folding pathway
Interacts with unfolded, misfolded, or partially folded
polypeptides
