Day 7 Flashcards
overall three dimensional arrangement of all th atoms in a protein
tertiary structure
what holds segments in position in tertiary structure
weak interactions and covalent bonds
arrangement of 2+ separate polypeptide chains in 3D complexes
quaternary structure
how many major types of proteins based on polypeptide chains
4a
arranged in long strands or sheets
fibrous proteins
folded into a spherical or globular shape
globular proteins
embedded in a hydrophobic lipid membranea
membrane proteins
lacking stable tertiary strucurres
intrinsically disordered proteins
givers strength and or flexibility to structure s
fibrous proteins
simple repeating element of secondary structure
fibrous proteins
example of right handed alpha helix
alpha kertatin
main protein in silk
fibroin
predominately beta sheets conformation
fibroin
what is fibroin rich n
alanine and glycine
what is fibroin stabilized by
hydrogen bonding and van der waals interactions
found in connective tissue
collagen
what is the secondary structure of collagen
left handed helix
what is tertiary and quaternary structure of collagen
right handed twisting of 3 separate polypeptides
what is caused by lack of vitamin C
scurvy
fold back on each other, more compact than fibrous proteins
globular proteins
enzymes, transport proteins, motor proteins, regulatory proteins, immunoglobins are all what
globular proteins
lack definable structure
instrinsically disordered proteins
often lack a hydrophobic core
intrinsically disordered proteins
high densities of charged residues and proline
intrinsically disordered proteins
motif = what
fold
recognizable folding pattern involving 2+ elements of secondary structure and the connections
motif/fold
assembly of multiple peptide subunits, what structure
quaternary structure
repeating structural unit
protomer
multisubunit protein
oligomer/multimer
loss of 3D structure sufficient to cause loss of function
denaturation
what can cause denaturation
heat, pH extremes, miscible solvents, certain solutes, detergents
what does denaturation often lead to
protein precipitation
process by which certain denatured globular proteins regain their native structure and biological activity
renaturation
can all proteins undergo renaturation
no
2 kinds of protein folding
spontaneous and assisted folding
based on amino acid r group interactions, what folding type
spontaneousg
guided by chaperone proteins
assisted folding
binds to hydrophobic regions
HSP 70
protein complexes assign in protein folding
chaperonins
misfolded protein
prion
what dictates protein function
structure of the protein
many proteins require what to function
binding to a ligand
anything that binds the protein at a specific site
ligand
protein functions can either be grouped as what or what
catalytic or noncatalytic
example of non catalytic protein functiosn
oxygen binding proteins like myoglobin and hemoglobin
what group do myoglobin and hemoglobin require
heme
consists of complex organic ring structure with a bound Fe2+ atom
heme
highly conserved tertiary structure with 8 alpha helical segments connected by bends
globins
most globes function in what
O2 transport or storage
153 residues and 1 molecule of heme
myoglobin
oxygen carrier in the muscle
myoglobin
