Learning about protein folding via potential functions
نویسندگان
چکیده
منابع مشابه
Learning about protein folding via potential functions.
Over the last few years we have developed an empirical potential function that solves the protein structure recognition problem: given the sequence for an n-residue globular protein and a collection of plausible protein conformations, including the native conformation for that sequence, identify the correct, native conformation. Having determined this potential on the basis of only some 6500 na...
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There has been a great deal of activity recently on approaches to the calculation of protein folding using specially devised empirical potential functions. We have developed one such function that solves the protein structure recognition problem: given the sequence for a globular protein and a collection of plausible protein conformations, including the native conformation for that sequence, id...
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The relationship between the optimization of the potential function and the foldability of theoretical protein models is studied based on investigations of a 27-mer cubic-lattice protein model and a more realistic lattice model for the protein crambin. In both the simple and the more complicated systems, optimization of the energy parameters achieves significant improvements in the statistical-...
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One of the most difficult problems in computational chemistry is the prediction of the three-dimensional structure of a protein molecule given only its amino acid sequence. Although there are several programs for calculating the empirical or quantum mechanical energies, and there are more programs for either minimizing the energy as a function of conformation or for simulating the dynamics of a...
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A new proof of Euler's formula for polytopes is presented via an approach using potential functions. In particular, a connection between Euler's formula and the Morse relation from differential topology is established.
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ژورنال
عنوان ژورنال: Proteins: Structure, Function, and Genetics
سال: 1994
ISSN: 0887-3585,1097-0134
DOI: 10.1002/prot.340200206