α-Helical, but not β-sheet, propensity of proline is determined by peptide environment

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

Volumn 93, Issue 13, 1996, Pages 6676-6681

  Li, Shun Cheng ^a,b,c   Goto, Natalie K ^a,b   Williams, Karen A ^a,b,d   Deber, Charles M ^a,b  

^a HOSPITAL FOR SICK CHILDREN RESEARCH INSTITUTE   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c MOUNT SINAI HOSPITAL   (Canada)

^d EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PROLINE;

AMINO ACID SEQUENCE; ARTICLE; GENE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; BASE SEQUENCE; CAPSID; CIRCULAR DICHROISM; HEAT; MEMBRANES, ARTIFICIAL; MICELLES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGOPEPTIDES; PORINS; PROLINE; PROTEIN CONFORMATION; SOLUTIONS; SOLVENTS; WATER;

EID: 0030015420     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.13.6676     Document Type: Article

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