Comparisons of interfacial phe, tyr, and trp residues as determinants of orientation and dynamics for GWALP transmembrane peptides

Biochemistry

Volumn 53, Issue 22, 2014, Pages 3637-3645

  Sparks, Kelsey A ^a   Gleason, Nicholas J ^a   Gist, Renetra ^a   Langston, Rebekah ^a   Greathouse, Denise V ^a   Koeppe, Roger E ^a  

^a UNIVERSITY OF ARKANSAS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANCHORS; AROMATIC COMPOUNDS; AROMATIZATION; FUNCTIONAL GROUPS; HYDROGEN BONDS; LIPID BILAYERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

AROMATIC AMINO ACID; HYDROPHOBIC RESIDUES; INTEGRAL MEMBRANE PROTEINS; MEMBRANE-WATER INTERFACE; PREFERRED ORIENTATIONS; SEPARATION DISTANCES; SOLID-STATE NMR SPECTROSCOPY; TRANSMEMBRANE HELICES;

ROTATION;

ALANINE; DILAUROYLPHOSPHATIDYLCHOLINE; DIOLEOYLPHOSPHATIDYLCHOLINE; MEMBRANE PROTEIN; PEPTIDE; PHENYLALANINE; TRYPTOPHAN; TYROSINE;

ALPHA HELIX; ARTICLE; BILAYER MEMBRANE; HYDROGEN BOND; LIPID BILAYER; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SOLID STATE;

MASS SPECTROMETRY; MEMBRANE PROTEINS; MOLECULAR DYNAMICS SIMULATION; PEPTIDE FRAGMENTS; PEPTIDES; PHENYLALANINE; TRYPTOPHAN; TYROSINE;

EID: 84902175608     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500439x     Document Type: Article

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