Prediction of rotational orientation of transmembrane helical segments of integral membrane proteins using new environment-based propensities for amino acids derived from structural analyses

FEBS Journal

Volumn 274, Issue 10, 2007, Pages 2653-2660

  Dastmalchi, Siavoush ^a,b   Beheshti, Samira ^b   Morris, Michael B ^c   Bret Church, W ^d  

^a TABRIZ UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^b TABRIZ UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^c UNIVERSITY OF ADELAIDE   (Australia)

^d UNIVERSITY OF SYDNEY   (Australia)

Author keywords

Lipid propensity; Membrane proteins; Molecular modeling; Transmembrane helix

Indexed keywords

MEMBRANE PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; MATHEMATICAL ANALYSIS; MOLECULAR MODEL; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; SOLUBILITY;

AMINO ACIDS; COMPUTER SIMULATION; HYDROPHOBICITY; MEMBRANE PROTEINS; PROTEIN FOLDING; ROTATION; SOLUBILITY; WATER;

EID: 34247585679     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05800.x     Document Type: Article

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