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Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 29, 2007, Pages 11963-11968

The design and characterization of two proteins with 88% sequence identity but different structure and function

(5) Alexander, Patrick A a He, Yanan a Chen, Yihong a Orban, John a Bryan, Philip N a

a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE (United States)

Author keywords

Evolution; Folding; NMR; Protein design; Protein structure

Indexed keywords

IMMUNOGLOBULIN G; PROTEIN G; PROTEIN GA; PROTEIN GB; SERUM ALBUMIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; HUMAN; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CIRCULAR DICHROISM; EPITOPES; HUMANS; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SERUM ALBUMIN; STREPTOCOCCUS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 34547499110 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.0700922104 Document Type: Article

Times cited : (160)

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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.