Predicting structures for genome proteins.

D Fischer; D Eisenberg

doi:10.1016/s0959-440x(99)80029-3

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PubMed · 10322219

Predicting structures for genome proteins.

D Fischer·D Eisenberg

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Abstract

Assigning three-dimensional protein folds to genome sequences is essential to understanding protein function. Although experimental three-dimensional structures are currently available for only a very small fraction of these sequences, computational fold assignment is able to assign folds to 20-30% of the sequences in various genomes. This percentage varies depending on the particular organism under analysis, on the sensitivities of the methods used and on the number of experimental structures available at the time the assignment is carried out. The fraction of assignable sequences is currently increasing at an annual rate of roughly 18%. If this rate is sustained throughout the coming years, three-dimensional computational models for more than half of the genome sequences may be available by the year 2003.

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Amino Acid Sequence Crystallization Genome, Human Humans Internet Models, Molecular Protein Conformation Protein Folding Proteins Sequence Homology, Amino Acid Journal Article Review

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D Fischer, D Eisenberg. 1999. Predicting structures for genome proteins.. https://doi.org/10.1016/s0959-440x(99)80029-3

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