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- W2125793518 abstract "The feasibility of determining the conformation of segments of polypeptide chain up to six residues in length in globular proteins by means of systematic search through the possibles conformations has been investigated. Trial conformations are generated by using representative sets of ϕ, ψ, and χ angels that have been derived from an examination of the distributions of these angles in refined protein structures. A set of filters based on simple rules that protein structures obey is used to reduce the number of conformations to a manageable total. The most important filters are the maintenance of chain integrity and the avoidance of tooshort van der Waals contacts with the rest of the protein and with other portions of the segment under construction. The procedure is intended to be used with approximate models so that allowance is made throughout for errors in the rest of the structure. All possible main chains are first constructed and then all possible side-chain conformations are built onto each of these. The electrostatic energy, including a solvent screening term, and the exposed hyrophobic area are evaluated for each accepted conformation. The method has been tested on two segments of chain in the trypsin like enzyme from Streptomyces griseus. It is found that there is a wide spread of energies among the accepted conformations, and the lowest energy ones have satisfactorily small root mean square deviations from the X-ray structure." @default.
- W2125793518 created "2016-06-24" @default.
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- W2125793518 date "1986-02-01" @default.
- W2125793518 modified "2023-10-16" @default.
- W2125793518 title "An algorithm for determining the conformation of polypeptide segments in proteins by systematic search" @default.
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- W2125793518 doi "https://doi.org/10.1002/prot.340010207" @default.
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