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52 Cards in this Set

  • Front
  • Back
proteins are composed of multiple _____ bonds.
amide
Where is protein stored?
casien
______ tranport hemoglobin.
proteins
structure of protein
collagen and keratin
_____ is the catalyst of a protein that decreases activation energy.
enzyme
_____ is the amino acid that doesn't fit the formula of having an amino group and an acid group, but still has a chiral center
proline
Are amino acids arranged as D's or L's?
L's
Where are the C-terminus (carboxylic acid) and N-terminus (amine) located on amino acids?
c- right
n- left
With the exception of _____, all protein-derived amino acids have at least 1 stereocenter (the alpha-carbon) and are chiral
glycine
The majority of alpha amino acids have the ___-configuration at the alpha-carbon.
L
If an amino acid is non-polar, it contains ______ on the R group
hydrocarbons
If an amino acid is polar but has neutral side chains, it contains ____ on the R group.
-OH or -SH
If an amino acid is acidic, it contains a ____ on the R group.
carboxylic acid
If an amino acid is basic, it contains a ___ on the R group.
amine
All 20 amino acids are ___ amino acids meaning they contain a chiral C with R group attached.
alpha
For 19 of the 20 amino acids, the alpha amino group is primary, for ____, it is secondary.
proline
Except ____, the alpha carbon of each amino acid is a stereocenter.
glycine
2 amino acids that contain a second amino acid
1) isoleucine
2) theonine
____ is a compound where both a positive charge and a negative charge exist on the same molecule.
Zwitterion
AA are ____ compounds.
ionic
Ionic nature changes depending on solution ___.
pH
__ is the "isoelectric point" (ph where AA or protein has no charge)
pl
What is the charge of pl on AA?
no charge
If a zwitterion is more acidic, there is excess ___.
H+
If a zwitterion is more basic, there is excess ____.
OH-
The -SH group of cysteine is easily oxidized to a ____.
disulfide
_____ is a secondary structure in which a section of polypeptide coils. (slinky)
alpha helix
____ is a secondary structure in which 2 polypeptide chains align parallel/antiparallel to each other. (noodles)
beta-pleated sheet
____ is tough and insoluble protein in which the chain form long fibers or sheet.
fibrous
____ structure is responsible for the structure of fibrous protein.
secondary
____ are water soluble proteins whose chains are folded into compact, globular shape with hydrophilic groups on the outside.
globular protein
multiple secondary=
tertiary
_____ stabilizes the 3-D structure of tertiary structure.
cross linking
How are tertiary structures held together?
h-bonds or disulfide bonds
_____ is a protein composed of only amino acid residues.
simple
_____ is a protein htat incorporated 1 or more non-amino acid units in its structure.
conjugated protein
______ is the arrangement of polypeptide chains into a noncovalently bonded aggregation. (only attracted)
quaternary structure
triple helix is an ex. of ____ structure
quaternary
Fetal hemoglobin has a greater affinity for ____ than does adult hemoglobin.
oxygen
_____ is a glycosidic bond between the saccharide and the OH goup of serine, thronine, or hydroxylysine.
O-linked saccharide
____ is an N-glycosidic bond between the anomeric carbon of N-acetyl-D-glucosamine and the nitrogen of the side chain amide group of asparagine.
N-linked saccharides
_____ is the loss of secondary, tertiary, or quaternary protein structure due to disruption of non-covalent interactions and or disulfide bonds that leaves peptide bonds and primary structure intact.
protein denaturation
____ is a denaturation that breaks down protein in food.
heat
Salt is a denaturation that changes _____.
pH
___ is a denaturation that breaks disulfide bonds.
reducing agent
Tenderizor is an ex. of denaturation for ___
agitation
acid/base denaturation is an ex. of _____
hydrolysis
Enzymes decrease activation energy, do they change equilibrium?
NO
____ is an enzyme classification of the addition of groups to a double bond, or removal of groups to create a double bond.
lyases
____ is an enzyme classification of the joining of 2 molecules.
ligases
the majority of enzyme activity is at what temp?
35-45
What is the optimal pH for enzyme activity?
6-7.5