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An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius.

ABSTRACT: We report a crystallographic and computational analysis of two mutant forms of the Alicyclobacillus acidocaldarius thioredoxin (BacTrx) done in order to evaluate the contribution of two specific amino acids to the thermostability of BacTrx. Our results suggest that the thermostability of BacTrx may be modulated by mutations affecting the overall electrostatic energy of the protein.

SUBMITTER: Bartolucci S

PROVIDER: S-EPMC164891 | biostudies-literature | 2003 Jul

REPOSITORIES: biostudies-literature

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An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius.

Bartolucci Simonetta S De Simone Giuseppina G Galdiero Stefania S Improta Roberto R Menchise Valeria V Pedone Carlo C Pedone Emilia E Saviano Michele M

Journal of bacteriology 20030701 14

We report a crystallographic and computational analysis of two mutant forms of the Alicyclobacillus acidocaldarius thioredoxin (BacTrx) done in order to evaluate the contribution of two specific amino acids to the thermostability of BacTrx. Our results suggest that the thermostability of BacTrx may be modulated by mutations affecting the overall electrostatic energy of the protein. ...[more]

PMID: 12837806

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