Structure of proteins III Flashcards
What affect do carbamates have on Hb
stabilize T state, promote O2 release
what happens when you reduce pH
promote O2 relase
what is the most common form of hemoglobin in adults
alpha2beta2 hemoglobin
what other type of Hb does adult blood contain
alpha2delta2
what is the predominate form of Hb in fetus during second and third trimester
alpha2gamma2
what is unique about HbF
histidine residency is replaced by serine, has incrased oxygen affinity
what is Hbsaki/Hbgenova
proline is introduced into an alpha-helical section
what is Hbcowtown
amino acid substituion destrabilizes the T form of molecule
methemoglobin
Fe2+ is oxidized to Fe3+
what substituion takes place in sickle cell
glutamate by valine
protein domain
substructure produced by any part of a polypeptide chain that can fold independently into a compact, stable structure
what are individual domains often connected by
flexible linkkers
what is collagen made up of
glycine
alanine
proline
hydroxyproline
what are the most abundant proteins in the body
collagen
what is collagen
glycoproteins of CT
what is the structure of collagen
triple helical units
how does the collagen helix twist
twists to the left, one turn every 3 residues
what is the repeating sequency of colalgen
gly - proline - hydroxyproline
where are glycine residues in tropocollagen
in the center, allowing a tight fit
how is the triple helix stabilized
interchain hydrogen bonds
how is hydroxyproline residues important in collagen
form additional hydrogen bonds, vital for stability
formation of hydroxyproline an dhydroxylysine requires what
Fe2+. ascorbate, and alpha ketoglutarate
what catalyzes the formation of hydroxyproline
prolyl hydroxylase
what is happening in scury
lack of ascorbate precents formation of hydroproline and hydrozylysine, so collagen can’t form stable helcies and CT is all fucked up
symptoms of scurby
leg pain, irritability, dry skin, bruising
osteogenesis imperfecta
brittle bone diseases
can be lethal, or the pt can barely notice it
