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• W2040594319 endingPage "238" @default.
• W2040594319 startingPage "227" @default.
• W2040594319 abstract "We describe the most general solution to date of the problem of matching globular protein sequences to the appropriate three-dimensional structure. The screening template, against which sequences are tested, is provided by a protein “structural fingerprint” library based on the contact map and the buried/exposed pattern of residues. Then, a lattice Monte Carlo algorithm validates or dismisses the stability of the proposed fold. Examples of known structural similarities between proteins having weakly or unrelated sequences such as the globins and phycocyanins, the eight-member αβ fold of triose phosphate isomerase and even a close structural equivalence between azurin and immunoglobulins are found." @default.
• W2040594319 created "2016-06-24" @default.
• W2040594319 creator A5010671148 @default.
• W2040594319 creator A5010808261 @default.
• W2040594319 creator A5025085688 @default.
• W2040594319 date "1992-09-01" @default.
• W2040594319 modified "2023-10-17" @default.
• W2040594319 title "Topology fingerprint approach to the inverse protein folding problem" @default.
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• W2040594319 doi "https://doi.org/10.1016/0022-2836(92)90693-e" @default.
• W2040594319 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1522587" @default.
• W2040594319 hasPublicationYear "1992" @default.
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