TAILIEUCHUNG - Báo cáo khoa học: Prediction of rotational orientation of transmembrane helical segments of integral membrane proteins using new environment-based propensities for amino acids derived from structural analyses

a-Helical integral-membrane proteins (IMPs) play a key role in many bio-logical processes, such as signal transduction, and are targets for 50% of current therapeutic drugs. In contrast to their significant abundance and biological importance, they comprise | ỊFEBS Journal Prediction of rotational orientation of transmembrane helical segments of integral membrane proteins using new environment-based propensities for amino acids derived from structural analyses Siavoush Dastmalchi1 2 Samira Beheshti2 Michael B. Morris3 and W. Bret Church4 1 Schoolof Pharmacy Tabriz University of MedicalSciences Tabriz Iran 2 Biotechnology Research Center Tabriz University of MedicalSciences Tabriz Iran 3 Australian Stem CellCentre ARC NHMRC Research Network in Genes and Environment in Development Schoolof Molecular and BiomedicalScience The University of Adelaide Australia 4 Faculty of Pharmacy University of Sydney Australia Keywords lipid propensity membrane proteins molecular modeling transmembrane helix Correspondence S. Dastmalchi Schoolof Pharmacy Tabriz University of MedicalSciences Daneshgah Street Tabriz 51664 Iran Fax 98 411 3344798 Tel 98 411 3372254 E-mail Received 28 November 2006 revised 18 February 2007 accepted 21 March 2007 doi a-Helical integral-membrane proteins IMPs play a key role in many biological processes such as signal transduction and are targets for 50 of current therapeutic drugs. In contrast to their significant abundance and biological importance they comprise 1 of structurally solved proteins. In the absence of experimental evidence molecular modeling of IMP structures is an alternative for providing structural information and aiding further experimental design. In the current work we propose two new amino acid lipid-facing propensity scales derived from the structural analysis of a nonredundant set of water-soluble proteins. The new scales p and Ỗ perform as well or better than published scales Carugo s hydrophobicity and kPROT scales in predicting the lipid-facing side of helical segments of a set of structurally solved IMPs thus indicating a that the folding properties of water-soluble proteins and IMPs are similar and b that the new scales will

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