Engineering a disulfide bond

Gabor E. Tusnady tusi at
Thu May 11 05:42:59 EST 2000


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.


Gabor E. Tusnady, PhD                   | e-mail:            tusi at
Institute of Enzymology, BRC            | www:
Hungarian Academy of Sciences           | tel:         (36-1) 466-6533/158
H-1113 Budapest Karolina ut 29, HUNGARY | fax:             (36-1) 466-5465

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.

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