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Re: [ccp4bb]: Thermostability vs Structure
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Hi Francisco,
I am afraid, your problem is close to unsolvable. The suggestions
that have been made so far are ok, but they deal with thermodynamic
aspects. From your email, however, it appears that you are looking at
the kinetics of protein unfolding. There is even less known about the
determinants of "kinetic stability" in proteins. Your observations
are absolutely in line with current concepts: most protein folding
experts would say that it is impossible to look at the native
structure of a protein and make inferences about its stability, or
how mutants might change its stability. I am afraid, the only way out
is to do a mutational analysis combined with a thorough thermodynamic
analysis.
Good luck,
Mischa
>I am dealing with a structure of an oxidase. I have relatively decent
>data till 1.7 A, and the model is practically refined. The protein is
>very thermostable with a half life of 2 hours at 80ºC.
>
>I have compared the structure with other "normal" oxidases, and I am not
>able to find suitable differences to explain thermostability in terms of
>structure. I have analyzed presence of disulfide bridges, salt bridges,
>packing , etc ..
>
>Is/was anybody dealing with a similar problem ?. What should be the
>factors to analyze for the explanation of thermostability ?
--
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Mischa Machius, PhD
Assistant Professor
University of Texas Southwestern Medical Center
Department of Biochemistry
5323 Harry Hines Blvd. Tel: +1 214 648 9760
L4.250 Fax: +1 214 648 8954
Dallas, TX 75390-9038, U.S.A. Email: Mischa.Machius@UTSouthwestern.edu
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