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Lecture

lecture5.docx

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Department
Biochemistry
Course Code
BIOC 212
Professor
Jason Young

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January 13, 2014 BIOC 212 Lecture 3 Continuation GroES: small GroEL: large Identical rings with alternate cyces Up, hydrophobicity = binding site for GroES Blank = no nucleotide How peptide is bound, where polypeptide substrate is folded Glucocorticoid Receptor N-terminal actives transcription LBD binds onto hormone -LBD w/out hormone is unstable, hydrophobic gap where hormone should be, cannot form stable folded state -LBD is dependent on chaperones all the time DNAJ binds to substrate, activates Hsc70 which also binds to substrate Hop links HSc70 and Hsp90 Lets go Hsc70, Hsp90 is still there, FKBP52 replaces HOP on Hsp90, together work on LBD, p23 stabilizes closed ATP bound form of Hsp90 -hormone should be present for stabilization -no hormone, keep on cycling until hormone is available Lecture 4 Heat Shock Response -for humans, heat shock is anything above 37 degrees C -even after cells are back to 37 degrees, translation is still inhibited (problem with unfolded proteins, don’t want to make more) HSF1 DNA binding domain: coloured yellow -only when HSF1 is a trimer, active form, can it recognize HSE promoters HSF Regulation Hsp90 is always cycling After heat shock, lots of unfolded proteins, a lot of hydrophobicity More HSF1 that is free and can bind excess Hsp90 Everything is in equilibrium Protein Modification -some side chains are more reactive than others, catalyzed by enzymes -surface proteins can be modified, induce a conformational change in proteins i.e. create a binding domain or block one -some modificatio
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