alpha-Helix dipole model and electrostatic stabilization of 4-alpha-helical proteins.
نویسندگان
چکیده
منابع مشابه
Designability of alpha-helical proteins.
A typical protein structure is a compact packing of connected alpha-helices and/or beta-strands. We have developed a method for generating the ensemble of compact structures a given set of helices and strands can form. The method is tested on structures composed of four alpha-helices connected by short turns. All such natural four-helix bundles that are connected by short turns seen in nature a...
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A minimal off-lattice model for α-helical proteins is presented. It is based on hydrophobicity forces and sequence independent local interactions. The latter are chosen so as to favor the formation of α-helical structure. They model chirality and α-helical hydrogen bonding. The global structures resulting from the competition between these forces are studied by means of an efficient Monte Carlo...
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Anfinsen's thermodynamic hypothesis implies that proteins can encode for stretching through reversible loss of structure. However, large in vitro extensions of proteins that occur through a progressive unfolding of their domains typically dissipate a significant amount of energy, and therefore are not thermodynamically reversible. Some coiled-coil proteins have been found to stretch nearly reve...
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Analysis of a database of structures of membrane proteins shows that membrane proteins composed of 10 or more transmembrane (TM) helices often contain buried helices that are inaccessible to phospholipids. We introduce a method for identifying TM helices that are least phospholipid accessible and for prediction of fully buried TM helices in membrane proteins from sequence information alone. Our...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1982
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.79.15.4545