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How does coding for antibodies work
Variable and constant portions are coded by seperate gene regions, then assembled on site in response to antigens. high mutation and mulitple assembly units allows for different variable proteins
DNA-binding proteins:
complexes that catalyize replication/transcription
homeodomain
largely-conserved protein that controls where body parts go during development - interacts with major groove for more chem info
coiled-coil motif (leucine zipper)
hydrophobic residues - binds to dna and proteins for dimerization
HLH proteins
helix-loop helix proteins
fibrous proteins
long fiber proteins, such as collagen, cytoskeleton fibrils
holdase
prevent collapse and aggregation of unfolded proteins, provide conditions for folding
foldase
catalyze folding/unfolding
Hsp70
heat shock protein 70 - working on polypeptide immediately when synthesis
DnaK
hsp70 in bacteria
hsp 40
assists hsp 70
co translational folding proteins
CCT, TCP-1, TriC in euks, GroEL and Gro-ES in proks: environment for folding
Modules in proteins to be folded
correspond to specific functional domains
ssa
viability and temperature protection
ssa2
nearly identical, constitutive
ssa1,3,4
divergent, heat shock inducible
ssb
non essential protein folding, both ssb1 and 2 are nearly identical and heat shock non-inducible
ssc
mitochondrial protection
kar2 and BiP
protection in ER
Ydj1
Hsp40 working with ssa
Zuo1
ssb hsp40: helped by Ssz1 (Hsp70)
Sis1
hsp40 working with ssa
RAC
ribosome associated chaperone complex - in yeast
ribosome, zuo1, ssb, ssz1, and NAC
NAC
nascent polypeptide associated complex: in RAC
Do mammalian cells contain orthologs of RAC system?
Nac and rac yes: zuo1 and ssz1, but not ssb
GroEL and GroES in bacteria
14 7×2 GroEl rings, GroES Lid
Describe the genes encoding euk and prok chaperonins
TCP-1, TriC and Cct have 8 subunits that are coded by different genes (CCT1-8): forms a double barrel ring with a cavity.
GroEL all by same
Euk/prok chaperonin binding behaviors?
Cct only binds a fraction of proteins while GroEL binds a all with nonpolar surface residues