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Re: [ccp4bb]: Thermostability vs Structure



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As stated by others, there appears to be no easily identified 
"structural design principles" to explain thermostability.  However, I 
saw a very interesting poster at a Gordon conference last year by Will 
Deutschman in Rick Dahlquist's lab that has just appeared in 
Biochemistry that uses careful thermodynamic studies and shows, at least 
for the studied proteins, the linkage of stability to increase in delta 
Cp of unfolding.  I think it's definitely worth looking at this paper.

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11669649&dopt=Abstract 
 

Francisco J. Enguita wrote:

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>
>Dear all :
>
>Sorry for posting this non-CCP4 question.
>
>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 ?
>
>Best regards
>
>Francisco
>
>
>
>============================================
>
>Francisco J. Enguita, Ph.D.
>Protein Crystallography laboratory
>Instituto de Tecnologia Química e Biológica
>Ap. 127
>2781-901 Oeiras
>PORTUGAL
>Phone : 351-21-4469669
>Fax : 351-21-4411277
>E-mail : fenguita@itqb.unl.pt
>
>============================================
>

-- 

David R. Buckler

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