Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues

Protein Science

Volumn 10, Issue 5, 2001, Pages 1023-1031

  Schwartz, R ^a   Istrail, S ^a   King, J ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Aggregation; Bioinformatics; Hydrophobic residues; Inclusion body; Sequence database

Indexed keywords

GLOBULAR PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; DATA BASE; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN AGGREGATION; SEQUENCE ANALYSIS;

ALKYL AND ARYL TRANSFERASES; AMINO ACIDS; ANIMALS; CAENORHABDITIS ELEGANS; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; CYTIDINE DEAMINASE; DATABASES; ESCHERICHIA COLI; GERANYLTRANSTRANSFERASE; LIPASE; MODELS, MOLECULAR; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PLANT PROTEINS; PROBABILITY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS; SACCHAROMYCES CEREVISIAE; UDPGLUCOSE-HEXOSE-1-PHOSPHATE URIDYLYLTRANSFERASE;

EID: 0035055990     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.33201     Document Type: Article

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