UMD BSCI 330 exam 2
the structure of secondary protein is dependent on? - ✔️✔️weak H-bonds b/t C=O & N-
H in backbone
- NOT SIDE CHAINS
the structure of beta sheet's is dependent on? - ✔️✔️H-bonding is between C=O & N-H
on ADJACENT polypeptide chains
with proteins, structure = - ✔️✔️function
describe the structure of primary proteins - ✔️✔️-linear sequence of amino acid residue
-determines mRNA structure
the structure of primary amino acids is dependent on? - ✔️✔️covalent binds b/t amino
acids in linear sequence
describe structure of secondary proteins - ✔️✔️-folding & twisting of peptide backbone
-NO amino acid side chain interactions
What are two well known structures of secondary proteins? - ✔️✔️-alpha helix
-beta helix
describe the structure of alpha helix - ✔️✔️-rigid cylindrical structure
-coils clockwise
the structure of alpha helix is dependent on? - ✔️✔️H-bonding between C=O & N-H
are 4 amino acids apart ON BACKBONE
4 amino acids = ___ helix turns - ✔️✔️ONE
describe the structure of beta sheet's - ✔️✔️-flat
-perpendicular interactions
in beta sheet's, adjacent polypeptide chains can be
___ OR ___ - ✔️✔️parallel or antiparallel
is the amino acid sequence of every protein identical to the genetically encoded primary
protein? - ✔️✔️NO! proteins get modified after translation
describe the structure of tertiary proteins - ✔️✔️3D arrangement of secondary structure
, the structure of tertiary protein is dependent on? - ✔️✔️noncovalent attraction between
R group & enviornment
describe the function(s) of disulfide bonds - ✔️✔️- help LOCK structure in place
-dont drive structure
Disulfide bonds in a protein chain connect - ✔️✔️2 cysteine residues
disulfide bonds only occur in ___ conditions. ex ___ enviornment - ✔️✔️-oxidative
conditions
- extracellular enviornments
what happens to disulfide bonds in reduction conditions? - ✔️✔️2 independent sulfides
in cytoplasm
unfolded state of proteins = - ✔️✔️lower free energy
folded state of proteins = - ✔️✔️higher free energy
proteins are more stable if G(unfolded) >/< G(folded) - ✔️✔️>
describe the function of molecular chaperones - ✔️✔️provide isolated chemical
enviornment for proteins to fold to FULL energy minimum
describe protein domains - ✔️✔️regions of protein that fold independently of other
regions. (removing doesnt affect)
can proteins only have 1 domain? - ✔️✔️no
What is a motif? ex? - ✔️✔️domain found in many relatd proteins
ex. DNA binding motif
describe the structure of quatenary proteins - ✔️✔️- composed of 1+ polypeptide chain
- multiple tertiary structures
the structure of quatenary protein is dependent on? - ✔️✔️R groups and enviornment
what are homomers? heteromers? - ✔️✔️homo: identical subunit polypeptide repeating
hetero: diff. subunit polypeptide (ex collagen)
T/F: Quatenary structures can be simple AND complex - ✔️✔️true
the structure of secondary protein is dependent on? - ✔️✔️weak H-bonds b/t C=O & N-
H in backbone
- NOT SIDE CHAINS
the structure of beta sheet's is dependent on? - ✔️✔️H-bonding is between C=O & N-H
on ADJACENT polypeptide chains
with proteins, structure = - ✔️✔️function
describe the structure of primary proteins - ✔️✔️-linear sequence of amino acid residue
-determines mRNA structure
the structure of primary amino acids is dependent on? - ✔️✔️covalent binds b/t amino
acids in linear sequence
describe structure of secondary proteins - ✔️✔️-folding & twisting of peptide backbone
-NO amino acid side chain interactions
What are two well known structures of secondary proteins? - ✔️✔️-alpha helix
-beta helix
describe the structure of alpha helix - ✔️✔️-rigid cylindrical structure
-coils clockwise
the structure of alpha helix is dependent on? - ✔️✔️H-bonding between C=O & N-H
are 4 amino acids apart ON BACKBONE
4 amino acids = ___ helix turns - ✔️✔️ONE
describe the structure of beta sheet's - ✔️✔️-flat
-perpendicular interactions
in beta sheet's, adjacent polypeptide chains can be
___ OR ___ - ✔️✔️parallel or antiparallel
is the amino acid sequence of every protein identical to the genetically encoded primary
protein? - ✔️✔️NO! proteins get modified after translation
describe the structure of tertiary proteins - ✔️✔️3D arrangement of secondary structure
, the structure of tertiary protein is dependent on? - ✔️✔️noncovalent attraction between
R group & enviornment
describe the function(s) of disulfide bonds - ✔️✔️- help LOCK structure in place
-dont drive structure
Disulfide bonds in a protein chain connect - ✔️✔️2 cysteine residues
disulfide bonds only occur in ___ conditions. ex ___ enviornment - ✔️✔️-oxidative
conditions
- extracellular enviornments
what happens to disulfide bonds in reduction conditions? - ✔️✔️2 independent sulfides
in cytoplasm
unfolded state of proteins = - ✔️✔️lower free energy
folded state of proteins = - ✔️✔️higher free energy
proteins are more stable if G(unfolded) >/< G(folded) - ✔️✔️>
describe the function of molecular chaperones - ✔️✔️provide isolated chemical
enviornment for proteins to fold to FULL energy minimum
describe protein domains - ✔️✔️regions of protein that fold independently of other
regions. (removing doesnt affect)
can proteins only have 1 domain? - ✔️✔️no
What is a motif? ex? - ✔️✔️domain found in many relatd proteins
ex. DNA binding motif
describe the structure of quatenary proteins - ✔️✔️- composed of 1+ polypeptide chain
- multiple tertiary structures
the structure of quatenary protein is dependent on? - ✔️✔️R groups and enviornment
what are homomers? heteromers? - ✔️✔️homo: identical subunit polypeptide repeating
hetero: diff. subunit polypeptide (ex collagen)
T/F: Quatenary structures can be simple AND complex - ✔️✔️true
