The relative positions of alanine residues in the hydrophobic core control the formation of two-stranded or four-stranded α-helical coiled-coils

Protein Engineering

Volumn 9, Issue 4, 1996, Pages 353-363

  Monera, Oscar D ^a   Sönnichsen, Frank D ^a   Hicks, Les ^a   Kay, Cyril M ^a   Hodges, Robert S ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Hydrophobic packing; Multiple helix coiled coil; Protein folding; helices

Indexed keywords

ALANINE; DISULFIDE; LEUCINE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; HYDROPHOBICITY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 0030003190     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/9.4.353     Document Type: Article

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