Uniformity, Ideality, and Hydrogen Bonds in Transmembrane α-Helices
نویسندگان
چکیده
منابع مشابه
Uniformity, Ideality, and Hydrogen Bonds in Transmembrane -Helices
Protein environments substantially influence the balance of molecular interactions that generate structural stability. Transmembrane helices exist in the relatively uniform low dielectric interstices of the lipid bilayer, largely devoid of water and with a very hydrophobic distribution of amino acid residues. Here, through an analysis of bacteriorhodopsin crystal structures and the transmembran...
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> < ABSTRACT: The intramolecular helix backbone C O H— N hydrogen Ž . bonding energies in poly L-alanine a helices have been estimated both in vacuum and in an aqueous environment using the parameter sets of five of the most commonly used force fields for modeling biomolecules, namely AMBER, CHARMM, ECEPP, GROMOS, and OPLS. The relative capabilities of these force fields in describing the H-bon...
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Alpha-helical transmembrane proteins mediate many key biological processes and represent 20–30% of all genes in many organisms. Due to the difficulties in experimentally determining their high-resolution 3D structure, computational methods that predict their topology (transmembrane helical segments and their orientation) are essential in advancing the understanding of membrane proteins’ structu...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2002
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(02)73969-6