Hi,
There was an article about the effect of the sequential environment of
cysteins to the disulfide forming potential of cysteins:
Fiser, A., Cserzo, M., Tudos, E., and Simon, I. (1992)
Different sequence environment of cysteins and half cystines in
proteins: Application to predict disulfide forming residues,
FEBS Letters 302, 117-120.
There is no html page or program, but using the table given in the article
you can easily calculate the potential of the disulfide forming.
Regards,
Gabor
Gabor E. Tusnady, PhD | e-mail: tusi at enzim.hu
Institute of Enzymology, BRC | www: http://www.enzim.hu/~tusi
Hungarian Academy of Sciences | tel: (36-1) 466-6533/158
H-1113 Budapest Karolina ut 29, HUNGARY | fax: (36-1) 466-5465
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At 10:21 PM 5/9/00 GMT, Larry wrote:
>My thesis work involves studying the protein-protein interactions
>between two enzymes. One of the interaction domains is a short 69
>amino acid coiled-coil motif. We've cloned and expressed this region
>in E. coli but want to engineer a disulfide bond to "close" off the
>loop (and make the motif more rigid). I know that disulfide bond formation
>is subject to many variables (correct phi, psi angles, etc.). Is
>there a computer or web-based program that will help me predict where
>I can insert two cysteines to create this disulfide bond? Thanks.
