Aromatic side-chain interactions in proteins. II. Near- and far-sequence Phe-X pairs

Proteins: Structure, Function and Genetics

Volumn 48, Issue 4, 2002, Pages 635-644

  Thomas, Annick ^a,b   Meurisse, Rita ^b   Brasseur, Robert ^b  

^a INSERM   (France)

^b UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

Aromatic pairs; Histidine; Phenylalanine; Secondary structures; Tryptophan; Tyrosine

Indexed keywords

HISTIDINE; META TYROSINE; PHENYLALANINE; TRYPTOPHAN;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; ARTICLE; GEOMETRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SEQUENCE ANALYSIS;

AMINO ACIDS, AROMATIC; ANIMALS; HISTIDINE; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PHENYLALANINE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SEQUENCE ANALYSIS, PROTEIN; TRYPTOPHAN; TYROSINE;

EID: 0036721415     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10191     Document Type: Article

References (9)

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7. Environment and exposure to solvent of protein atoms. Lysozyme and insulin
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