Ionic interactions promote transmembrane helix-helix association depending on sequence context

Journal of Molecular Biology

Volumn 396, Issue 2, 2010, Pages 452-461

  Herrmann, Jana R ^a,b   Fuchs, Angelika ^a   Panitz, Johanna C ^a,b   Eckert, Thomas ^a,b   Unterreitmeier, Stephanie ^a,b   Frishman, Dmitrij ^a   Langosch, Dieter ^a,b  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b Munich Center for Integrated Protein Science   (Germany)

Author keywords

GxxxG motif; Heterotypic; Ionic interaction; ToxR POSSYCCAT; Transmembrane domain

Indexed keywords

MEMBRANE PROTEIN; ION; MUTANT PROTEIN; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; COMBINATORIAL LIBRARY; CONTROLLED STUDY; IONIC STRENGTH; MOLECULAR CLONING; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN MOTIF; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; AMINO ACID SUBSTITUTION; CHEMISTRY; CONSENSUS SEQUENCE; ENZYME SPECIFICITY; GENETICS; METABOLISM; METHODOLOGY; PHYSIOLOGY; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CONSENSUS SEQUENCE; IONS; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 77449104569     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.11.054     Document Type: Article

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