Energy Functions for Protein Design: Adjustment with Protein–Protein Complex Affinities, Models for the Unfolded State, and Negative Design of Solubility and Specificity-Reference-Cited by-同舟云学术

Energy Functions for Protein Design: Adjustment with Protein–Protein Complex Affinities, Models for the Unfolded State, and Negative Design of Solubility and Specificity

Published:2005-03 Issue:1 Volume:347 Page:203-227
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Pokala Navin,Handel Tracy M.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference127 articles.

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4. Effective scoring function for protein sequence design;Liang;Proteins: Struct. Funct. Genet.,2004

5. Native protein sequences are close to optimal for their structures;Kuhlman;Proc. Natl Acad. Sci. USA,2000

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