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Evolutionary similarity among peptide segments is a basis for prediction of protein folding
Author(s) -
Sweet Robert M.
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360250813
Subject(s) - basis (linear algebra) , sequence (biology) , chemistry , similarity (geometry) , folding (dsp implementation) , protein primary structure , protein secondary structure , protein structure , protein folding , structural similarity , protein structure prediction , computational biology , peptide sequence , artificial intelligence , computer science , biochemistry , biology , mathematics , geometry , gene , electrical engineering , image (mathematics) , engineering
Short segments of polypeptide, from a protein for which the primary sequence but not the three‐dimensional structure is known, are compared to a library of known structures. The basis of comparison is the probability with which residues in the unknown segment might substitute through evolution for residues in segments of known structure. In test cases, segments from known structures that are similar in sequence to those from a protein treated as unknown are often found to be similar in three‐dimensional structure to one another and to the true structure of the “unknown” segment. This provides a basis for prediction of the local configuration (secondary structure) of polypeptides.