Helix kinks are equally prevalent in soluble and membrane proteins

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 9, 2014, Pages 1960-1970

  Wilman, Henry R ^a   Shi, Jiye ^b   Deane, Charlotte M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UCB PHARMA   (Belgium)

Author keywords

Helix bend; Helix distortion; Helix kink; Membrane protein; Protein helix; Protein structure; Soluble protein

Indexed keywords

ASPARAGINE; GLYCINE; MEMBRANE PROTEIN; PHENYLALANINE; PROLINE; PROTEIN; SERINE; THREONINE; TRYPTOPHAN; TYROSINE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; HELIX KINK; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MEMBRANE PROTEINS; MODELS, MOLECULAR; PROLINE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84906303304     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24550     Document Type: Article

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