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      I-TASSER server for protein 3D structure prediction.

      Author(s): 1
      Publication date (Electronic):
      Journal: BMC bioinformatics
      Publisher: Springer Science and Business Media LLC

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          Abstract

          Prediction of 3-dimensional protein structures from amino acid sequences represents one of the most important problems in computational structural biology. The community-wide Critical Assessment of Structure Prediction (CASP) experiments have been designed to obtain an objective assessment of the state-of-the-art of the field, where I-TASSER was ranked as the best method in the server section of the recent 7th CASP experiment. Our laboratory has since then received numerous requests about the public availability of the I-TASSER algorithm and the usage of the I-TASSER predictions.

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          Most cited references25

          • Record: found
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          Identification of common molecular subsequences.

          T.F. Smith, M.S. Waterman (1981)
          Article 0 comments Cited 1721 times – based on 0 reviews     Review now
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            A solution for the best rotation to relate two sets of vectors

            W Kabsch (1976)
            Article 0 comments Cited 472 times – based on 0 reviews     Review now
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              Protein structure prediction and structural genomics.

              D. Baker, A. Sali (2001)
              Genome sequencing projects are producing linear amino acid sequences, but full understanding of the biological role of these proteins will require knowledge of their structure and function. Although experimental structure determination methods are providing high-resolution structure information about a subset of the proteins, computational structure prediction methods will provide valuable information for the large fraction of sequences whose structures will not be determined experimentally. The first class of protein structure prediction methods, including threading and comparative modeling, rely on detectable similarity spanning most of the modeled sequence and at least one known structure. The second class of methods, de novo or ab initio methods, predict the structure from sequence alone, without relying on similarity at the fold level between the modeled sequence and any of the known structures. In this Viewpoint, we begin by describing the essential features of the methods, the accuracy of the models, and their application to the prediction and understanding of protein function, both for single proteins and on the scale of whole genomes. We then discuss the important role that protein structure prediction methods play in the growing worldwide effort in structural genomics.
              Article 0 comments Cited 336 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (iso-abbrev): BMC Bioinformatics
                Title: BMC bioinformatics
                Publisher: Springer Science and Business Media LLC
                ISSN (Electronic): 1471-2105
                ISSN (Print): 1471-2105
                Publication date (Electronic): Jan 23 2008
                Volume: 9
                Affiliations
                [1 ] Center for Bioinformatics and Department of Molecular Bioscience, University of Kansas, 2030 Becker Dr, Lawrence, KS 66047, USA. yzhang@ku.edu
                Article
                Publisher Item ID: 1471-2105-9-40
                DOI: 10.1186/1471-2105-9-40
                PMC ID: 2245901
                PubMed ID: 18215316
                SO-VID: 16df0fcf-8958-4da2-9b92-61d415d83be4
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