Folding of β/α-unit scrambled forms of S. cerevisiae triosephosphate isomerase: Evidence for autonomy of substructure formation and plasticity of hydrophobic and hydrogen bonding interactions in core of (β/α)8-barrel-Reference-Cited by-同舟云学术

Folding of β/α-unit scrambled forms of S. cerevisiae triosephosphate isomerase: Evidence for autonomy of substructure formation and plasticity of hydrophobic and hydrogen bonding interactions in core of (β/α)8-barrel

Published:2004-04-01 Issue:3 Volume:55 Page:548-557
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Shukla Anshuman,Guptasarma Purnananda

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference24 articles.

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4. Characteristics of a de novo designed protein;Tanaka;Protein Sci,1994

5. Nucleotide sequence of the triose phosphate isomerase gene of Saccharomyces cerevisiae;Alber;J Mol Appl Genet,1982

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