> Hello PPS-mates,
>
> I would like to understand the role of the
> aspartic acid residue in the catalytic triad
> (asp,his,ser) of trypsin/ogen. I understand what the
> his and ser are doing during the peptide cleaving, but I
> have not been able to figure out what the asp does? Can
> someone explain this?
>
> Thanks...
>
Hi Gail,
This goes for chymotrypsin's triad. Generally asp orients the imidazole
ring of his, and partly neutralizes the charge that develops during the
transition state. Look up Stryer's Biochemistry, 3rd ed. pp224-226
Hope this helped.
Iddo
_____________________________________________________________________________
Iddo Friedberg |
|
email: idoerg@shum.cc.huji.ac.il | "Mein Gott! They've got tails!"
|
Snail: Iddo Friedberg | - comment on first EM photograph
Dept. of Biological Chemistry | of a bacteriophage. 1942
Life-Sciences Institute |
The Hebrew University |
Jerusalem, Israel |
|
Phone : (972)-2-6585459 |
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