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

Volumn 98, Issue 25, 2001, Pages 14340-14344

Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants

(2) Fleming, Karen G a Engelman, Donald M b

a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE (United States)

b YALE UNIVERSITY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; DIMER; GLYCINE; GLYCOPHORIN A;

ARTICLE; DIMERIZATION; ENERGY TRANSFER; HYDROPHOBICITY; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; ULTRACENTRIFUGATION;

BINDING SITES; DIMERIZATION; DRUG STABILITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOPHORIN; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; THERMODYNAMICS; ULTRACENTRIFUGATION; VARIATION (GENETICS);

EID: 0035807810 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.251367498 Document Type: Article

Times cited : (165)

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