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J Comput Biol. 1995 Spring;2(1):125-38.

Algorithms for protein structural motif recognition.

Author information

1
Mathematics Department, Massachusetts Institute of Technology, Cambridge 02139, USA.

Abstract

The identification of protein sequences that fold into certain known three-dimensional (3D) structures, or motifs, is evaluated through a probabilistic analysis of their one-dimensional (1D) sequences. We present a correlation method that runs in linear time and incorporates pairwise dependencies between amino acid residues at multiple distances to assess the conditional probability that a given residue is part of a given 3D structure. This method is generalized to multiple motifs, where a dynamic programming approach leads to an efficient algorithm that runs in linear time for practical problems. By this approach, we were able to distinguish (2-stranded) coiled-coil from non-coiled-coil domains and globins from nonglobins. When tested on the Brookhaven X-ray crystal structure database, the method does not produce any false-positive or false-negative predictions of coiled coils.

PMID:
7497115
DOI:
10.1089/cmb.1995.2.125
[Indexed for MEDLINE]

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