Week 2 Richter ILA's Flashcards
proteins that use highly frequent codons get expressed at what rate
a higher rate
this translocation mutation causes leukemia
chromsome 22 to 9
Philadelphia chromosome
mutation that does not change function of protein
silent
mutation that changes function of protein
missense
mutation that causes termination of protein
nonsense
Purines
A and G
Pyrimidines
C, U, T
example of missense mutation where there is a deletion of 508 on CFTR gene
CF (cystic fibrosis)
amino acid sequence makes up what structure
primary
alpha helix
beta sheet
secondary
alpha helix and beta sheets together
tertiary
multiple amino acid chains assembled together (2 alpha helix and beta sheets)
quaternary
partial double bond
rigid, planar
trans-configuration
uncharged; polar
peptide bond
most important structural motif in proteins
alpha helix
which amino acids prefer helix
MALEK
what bonding is important for alpha helix
intra-chain H bonding
what bonding is important for beta sheets
interchain H bonding
which amino acids are found in beta sheets
aromomatic residues
(tyr, phe, trp)
what bonding is important for tertiary structure
H bonding of side chains
transcription factor that is a homodimer and held together by hydrophobic faces of parallel Leu zippers
Leu zipper (bZIP)
transcription factor that has its domain in MyoD (essential for muscle development)
bHLH (basic helix-loop-helix)
calcium binding happens in the loop region of what motif
helix-loop-helix
example of beta barrel
porins (antibiotics)
happens from accumulation of misfolded proteins (plaques of Tau); amyloid abeta
Alzheimer’s disease
infectious agent that cause misfolding of the normal form of the protein (PrPc)
Prion proteins (PrPSc)
oxygen saturated Hb
in the lungs
oxygen free Hb
in the tissues
(Hb gives off oxygen to myoglobin in tissues and myoglobin will bind until it is time to contract muscle)
oxygen saturation curve for myoglobin is left shifted: what does that mean?
higher affinity than hemoglobin
oxygen saturation curve for hemoglobin is sigmoidal: why
sigmoidal suggests cooperativity b/t subunits (the more O2 that binds, increases O2 affinity)
when pH lowers, where does oxygen saturation curve shift
to the right
(less affinity means hemoglobin will give off O2 easier, and thats what you want to happen in tissues)
what will increased 2,3-BPG do to curve
shift to the right
(blood from individuals adapted to high altitudes-more glycolysis and less affinity for O2 so it can be released)
main affect of carbon monoxide on oxygen saturation curve
occupies Hb and prevents O2 from binding (total capacity of O2 is reduced vertically)
predominant form of Hb
HbA
form of Hb induced by sickle cell anemia
HbF
form of Hb induced by thalassemias
HbA2
form of Hb increased in diabetics; proportional to blood glucose in the body
HbA1c
extracellular fibrous proteins
collagen and elastin
main part of collagen structure
alpha chain
(quaternary structure-3 chains linked together)
cleavage of N and C terminus of procollagen happens where
extracellular space
striated look of collagen is simply the what
collagen fibril regions
