Exam 2 proteins Flashcards
what are the 4 types of globular proteins?
all a, all b, a/b, little secondary structure
proteins with little secondary structure function by _____
binding with other molecules
what is the most typical globular shape?
a/b
___ ____ are amino acid sequences that are used repeatedly in the same protein or are found in different proteins
protein domains
protein domains are typically __ to ___ amino acids long
40, 100
do protein domains have the same or different function in different proteins?
different
what are the two ways that protein domains are formed?
duplication of DNA segments within a gene, insertion of a DNA segment into another gene
some domains are ____ and their function is unknown
neutral
domains ____ over time and do not resemble the original
mutate
what is the first step of protein folding?
new polypeptide forms segments of secondary structure, either a helix or beta sheets
a helix and b sheet formation is due to what type of bonding?
hydrogen
what is the second step of protein folding?
secondary structures form a globular shape
how is a globular shape aquired?
through hydrophobic interactions
what is the third step of protein folding?
tertiary structure is generated by adjustments to the folded structure
____ ____ are proteins in the cell that bind new proteins and help bring parts together to get the proper 3D folding
molecular chaperones
the intermediates of protein folding involve __-___ __ ___
R-side chain interactions
____ ____ are misfolded, insoluble and aggregated proteins in brain cells
amyloid deposits
what protein is misfolded in Alzheimer’s Disease?
amyloid-b
what protein is misfolded in Parkinson’s Disease?
s synuclein
___ and ____ are produced via the same type of forces
tertiary, quaternary
quaternary structure allows for __ ____ between subunits of proteins
cooperative behavior
how does hemoglobin exhibit cooperative behavior?
the binding of the first O2 molecule makes it easier for the 3 other O2 molecules to each bind to a subunit
nitrite reductase, fumarase, hemoglobin, and methane hydroxylase all have what type of quaternary structure?
fixed number of subunits
microtubules have what type of quaternary structure?
open
___ ___ polymerize to form microtubules
tubulin dimers
folding of a newly synthesized protein into the final 3D structure primarily involves the interactions of what?
amino acid side chains
a protein has quaternary structure if it has more than ____ polypeptide chain
1
_____ primarily hold together tertiary and quaternary structure
hydrophobic
what 3 things hold together tertiary and quaternary structure?
hydrophobic interactions, hydrogen bonds, and ionic interactions
____ ______ are when the interacting surfaces are identical and the resulting structure is dimeric
isologous interactions
____ ______ involve nonidentical interfaces, and the surfaces must be complementary
heterologous associations
reducing the protein’s surface to volume ratio increases its ____
stability
what are the 4 benefits of quaternary association?
stability, genetic economy/efficiency, catalytic sites coming together, cooperativity