Beta-branched residues adjacent to GG4 motifs promote the efficient association of glycophorin A transmembrane helices.

Biopolymers

Volumn 96, Issue 3, 2011, Pages 340-347

  Cunningham, Fiona ^a   Poulsen, Bradley E ^b   Ip, Wilfred ^b   Deber, Charles M ^b  

^a HOSPITAL FOR SICK CHILDREN RESEARCH INSTITUTE   (Canada)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPHORIN; RECOMBINANT PROTEIN;

ARTICLE; CELL MEMBRANE; CHEMISTRY; ESCHERICHIA COLI; GENETICS; HUMAN; METABOLISM; MISSENSE MUTATION; PHYSIOLOGY; PROTEIN MOTIF; PROTEIN MULTIMERIZATION;

AMINO ACID MOTIFS; CELL MEMBRANE; ESCHERICHIA COLI; GLYCOPHORIN; HUMANS; MUTATION, MISSENSE; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS;

EID: 80052898060     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.21565     Document Type: Article

References (0)