Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition-Reference-Cited by-同舟云学术

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Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition

Published:2006-04-19 Issue:11 Volume:580 Page:2646-2652
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Sivakumar Neelamegam,Li Nan,Tang Julian W.,Patel Bharat K.C.,Swaminathan Kunchithapadam

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference25 articles.

1. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability;Vieille;Appl. Environ. Microbiol.,1995

2. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution;Russell;Biochemistry,1997

3. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2;Perutz;Nature,1975

4. The stability of proteins in extreme environments;Jaenicke;Curr. Opin. Struct. Biol.,1998

5. Halophilic adaptation of enzymes;Madern;Extremophiles,2000

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