Studied by 63 Peopletrypsin
Tags & Description
trypsin
what enzyme cuts chains after arginine and lysine?
cyanogen bromide
what compound cuts peptide chains after met?
true
true or false: an amino acid sequence will fold the same way every time it is produced if the conditions remain the same
primary
the amino acid sequence is the __________ level of protein structure
secondary
the local folding (helix, sheet) of a peptide chain is the ___________ level of protein structure
tertiary
the overall folding of an amino acid is the ___________ level of protein structure
quaternary
the association of different subunits is the __________ level of protein structure
supersecondary structure
groupings of different secondary structures is referred to as the ________________
alpha helix
two negative angles of phi and psi on a Ramachandran diagram
beta sheet
positive and negative angles of phi and psi on a Ramachandran diagram
3.6
alpha helices have how many residues per turn?
true
true or false: max spacing of r groups and hydrogen bonds contribute to the energetically stable forms of both alpha helices and beta sheets
proline
beta hairpin turns have 2-4 amino acids with at least 2 of them being _________
pH, temperature, denaturing chemicals, ionic strength, redox
factors that affect protein stability
decrease
salting in causes a(n) _____________ in stability
increase
salting out causes a(n) ____________ in stability
true
true or false: some proteins require a chaperonin such as GroEl in order to fold correctly
beta sheet, alpha helix
PrP-Sc represents the misfolded form of PrP-c. the misfolded version has more _________ than ____________
adenylate cyclase
activated g protein moves along the membrane to reach an effector molecule, such as ___________
trimeric
g proteins usually have 3 subunits, making them _________ in nature
first messenger
g protein signaling mechanisms are usually initiated by a _______________
humoral immunity
immune response involving antigens binding directly to B cells, causing the production of antibodies
cell mediated immunity
immune response involving the destruction of infected cells by cytotoxic T cells, or the destruction of intracellular pathogens by macrophages
collagen
every third amino acid is gly
alpha keratin
every fourth residue is hydrophobic
fibroin
common sequence is gly-ala or gly-ser, which allows close packing
elastin
rich in glycine, alanine, and valine
ca, troponin
the binding of ____ to ______ results in the movement of tropomyosin and the exposure of the myosin binding site on the actin filament
directly
at low substrate concentration, the rate of reaction would be ___________ proportional to the substrate concentration
competitive inhibitors
affect the value of Km and not Vmax
Km
describes the affinity of an enzyme for a substrate
Km
substrate concentration required to reach 1/2 the max velocity
Km
describes the stability of the ES complex
Km
= (K1 + K2)/k1
lock and key enzyme
active site is specific to the substrate, thereby enhancing forward momentum in the reaction progress
stabilized
the transition state of an enzyme and substrate reaction is ___________ by the specificity of the active site for the substrate
covalent
serine at the active site of serine proteases provides _______ catalysis
acid base
histidine residue in a serine protease provides __________ catalysis
proximity effects
_____________ can be caused by site specificity, can be enhanced by substrate channeling, result in an increased effective concentration of substrate, and function to lower the energy of activation