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...
متن کاملStructural determinants of transmembrane helical proteins.
We identify a structural feature of transmembrane helical proteins that restricts their conformational space and suggests a new way of understanding the construction and stability of their native states. We show that five kinds of well-known specific favorable interhelical interactions (hydrogen bonds, aromatic interactions, salt bridges, and two interactions from packing motifs) precisely dete...
متن کاملA Minimal Off-Lattice Model for Alpha-helical Proteins
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...
متن کاملAb initio molecular-replacement phasing for symmetric helical membrane proteins
Obtaining phases for X-ray diffraction data can be a rate-limiting step in structure determination. Taking advantage of constraints specific to membrane proteins, an ab initio molecular-replacement method has been developed for phasing X-ray diffraction data for symmetric helical membrane proteins without prior knowledge of their structure or heavy-atom derivatives. The described method is base...
متن کاملTopology prediction for helical transmembrane proteins at 86% accuracy.
Previously, we introduced a neural network system predicting locations of transmembrane helices (HTMs) based on evolutionary profiles (PHDhtm, Rost B, Casadio R, Fariselli P, Sander C, 1995, Protein Sci 4:521-533). Here, we describe an improvement and an extension of that system. The improvement is achieved by a dynamic programming-like algorithm that optimizes helices compatible with the neura...
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ژورنال
عنوان ژورنال: Nature
سال: 1989
ISSN: 0028-0836,1476-4687
DOI: 10.1038/337204a0