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A short survey on protein blocks.

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  • Additional Information
    • Contributors:
      Dynamique des Structures et Interactions des Macromolécules Biologiques (DSIMB); Institut National de la Transfusion Sanguine Paris (INTS)-Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM); Molecular Biophysics Unit; Indian Institute of Science (IISc); National Centre for Biological Sciences TIFR (NCBS); Tata Institute for Fundamental Research (TIFR); Dynamique des Structures et Interactions des Macromolécules Biologiques - Pôle de La Réunion (DSIMB Réunion); Biologie Intégrée du Globule Rouge (BIGR (UMR_S_1134 / U1134)); Institut National de la Transfusion Sanguine Paris (INTS)-Université Paris Diderot - Paris 7 (UPD7)-Université de La Réunion (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université des Antilles (UA)-Institut National de la Transfusion Sanguine Paris (INTS)-Université Paris Diderot - Paris 7 (UPD7)-Université de La Réunion (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université des Antilles (UA); Computational Biology Branch; NLM-NCBI; Laboratoire de physiologie cellulaire végétale (LPCV); Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG); Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA); Institute of Biotechnology AS CR; These works were supported by grants from the French Ministry of Research, University of Paris Diderot - Paris 7, University of Saint-Denis de la Réunion, French National Institute for Blood Transfusion (INTS), French National Institute for Health and Medical Research (INSERM) and Indian Department of Biotechnology. APJ and GA are supported by CEFIPRA number 3903-E and Council of Scientific and Industrial Research, respectively. AB had a grant from the French Ministry of Research, MT has a post-doctoral fellowship from NIH and HV had a post-doctoral fellowship from CEA. NS and AdB acknowledge to CEFIPRA for collaborative grant (number 3903-E). BS and AdB acknowledge to Partenariat Hubert Curien Barrande (2010-2011).
    • Publication Information:
      CCSD
    • Publication Date:
      2010
    • Collection:
      Université de la Réunion: HAL
    • Abstract:
      International audience ; Protein structures are classically described in terms of secondary structures. Even if the regular secondary structures have relevant physical meaning, their recognition from atomic coordinates has some important limitations such as uncertainties in the assignment of boundaries of helical and β-strand regions. Further, on an average about 50% of all residues are assigned to an irregular state, i.e., the coil. Thus different research teams have focused on abstracting conformation of protein backbone in the localized short stretches. Using different geometric measures, local stretches in protein structures are clustered in a chosen number of states. A prototype representative of the local structures in each cluster is generally defined. These libraries of local structures prototypes are named as "structural alphabets". We have developed a structural alphabet, named Protein Blocks, not only to approximate the protein structure, but also to predict them from sequence. Since its development, we and other teams have explored numerous new research fields using this structural alphabet. We review here some of the most interesting applications.
    • Relation:
      info:eu-repo/semantics/altIdentifier/pmid/21731588; PRODINRA: 246294; PUBMED: 21731588
    • Accession Number:
      10.1007/s12551-010-0036-1
    • Online Access:
      https://inserm.hal.science/inserm-00512823
      https://inserm.hal.science/inserm-00512823v1/document
      https://inserm.hal.science/inserm-00512823v1/file/inserm-00512823_edited.pdf
      https://inserm.hal.science/inserm-00512823v1/file/Joseph_Agarwal_BiohysRev_2010_preprint.pdf
      https://doi.org/10.1007/s12551-010-0036-1
    • Rights:
      info:eu-repo/semantics/OpenAccess
    • Accession Number:
      edsbas.EDBB9488