Residue patterning in helix interiors

Biochemistry and Cell Biology

Volumn 88, Issue 2, 2010, Pages 325-337

  Wathen, Brent ^a   Jia, Zongchao ^a  

^a QUEEN S UNIVERSITY   (Canada)

Author keywords

Amphipathicity; Helices; Hydrophobicity; Protein folding; Residue propensities

Indexed keywords

PROTEIN FOLDING;

AMPHIPATHIC; AMPHIPATHICITY; DATA SETS; HELICES; HELIX FORMATION; HYDROPHILICS; HYDROPHOBICS; NEGATIVE CORRELATION; POLAR RESIDUES; SIDE CHAINS; SIDE-CHAIN INTERACTIONS; STRUCTURAL ENVIRONMENT; TERTIARY INTERACTIONS; THEORETICAL STUDY;

HYDROPHOBICITY;

ARGININE; ASPARAGINE; ASPARTIC ACID; CYSTEINE; GLUTAMIC ACID; GLYCINE; HISTIDINE; ISOLEUCINE; LEUCINE; LYSINE; MEMBRANE PROTEIN; PHENYLALANINE; PROLINE; SERINE; TRYPTOPHAN; VALINE; PROTEIN;

ALPHA HELIX; CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; CORRELATION FUNCTION; HYDROPHILICITY; HYDROPHOBICITY; MOLECULAR EVOLUTION; MOLECULAR RECOGNITION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY; CHEMICAL PHENOMENA; CHEMISTRY; MOLECULAR DYNAMICS; PROTEIN DATABASE;

DATABASES, PROTEIN; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR DYNAMICS SIMULATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 77950597904     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O09-156     Document Type: Conference Paper

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