Charged single α-helix: A versatile protein structural motif

Proteins: Structure, Function and Bioinformatics

Volumn 74, Issue 4, 2009, Pages 905-916

  Süveges, Dániel ^a   Gáspári, Zoltán ^a   Tóth, Gábor ^b   Nyitray, László ^a  

^a EÖTVÖS LORÁND UNIVERSITY   (Hungary)

^b SZENT ISTVÁN UNIVERSITY   (Hungary)

Author keywords

Circular dichroism spectroscopy; Coiled coil; Fourier transformation; Intrinsically disordered proteins; Myosin; Protein kinase; Salt bridges; Structure prediction

Indexed keywords

MYOSIN VI; PROTEIN KINASE; WATER; PROTEIN;

ALGORITHM; ALPHA HELIX; AMINO ACID SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CHARGED SINGLE ALPHA HELIX; CIRCULAR DICHROISM; CONTROLLED STUDY; FOURIER TRANSFORMATION; PRIORITY JOURNAL; PROTEIN DATABASE; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; DATABASES, PROTEIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 61449257376     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22183     Document Type: Article

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