Kabsch, W., Sander, C. On the use of sequence homologies to predict protein structure: Identical pentapeptides can have completely different conformations. Proc. Natl. Acad. Sci. U.S.A. 81:1075--1078, 1984. Home/Search Document Not in Database Summary Related Articles Check |
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Synthesizing Regularity Exposing Attributes in Large Protein.. - Maza (1993) (4 citations) (Correct)
....j. Branden and Tooze [Branden and Tooze, 1991] group amino acids into four categories. Database scans have shown that there are identical pentapeptides that have different secondary structures assigned to the middle residue, but that there are no identical heptapeptides that have the same property [Kabsch and Sander, 1984, Argos, 1990] So, an estimate for the number of neighborhoods is: 4 7 = 16384. Of the three estimates, this one has the least support. Substituting these choices for the three parameters into 2.5: P total = 1 Gamma (1 Gamma 1=16384) 10000 (1 Gamma 1=16384) 10000 :54 = 7502 (2:6) ....
....decreasing the number of literals in a monomial. What is the justification for doing so Database searches show that there are identical pentapeptides that have different secondary structures assigned to the middle residue, but that there are no identical heptapeptides that have the same property [Kabsch and Sander, 1984, Argos, 1990] If this property holds for all proteins and not just those that exist in current databases, then 7 DNF formulae can be used to describe secondary structures. Although this reduces the number of instances needed to about 10 20 , far too many instances are still required. The ....
Kabsch, W. and Sander, C. (1984). On the use of sequence homologies to predict protein structure: Identical pentapeptides have completely different conformations. Proceedings of the National Academy of Science, 81:1075--1078.
Patterns, Structures, andAmino Acid Frequencies in.. - Fetrow, Palumbo, Berg (Correct)
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Kabsch, W., Sander, C. On the use of sequence homologies to predict protein structure: Identical pentapeptides can have completely different conformations. Proc. Natl. Acad. Sci. U.S.A. 81:1075--1078, 1984.
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