• DocumentCode
    2232060
  • Title

    RRM designed α-chymotrypsin-like peptides

  • Author

    Lazoura, Eliada ; Cosic, Irena

  • Author_Institution
    Dept. of Electr. & Comput. Syst. Eng., Monash Univ., Vic., Australia
  • fYear
    1998
  • fDate
    15-18 Feb 1998
  • Firstpage
    93
  • Lastpage
    94
  • Abstract
    The Resonant Recognition Model (RRM) has been applied to chymotrypsin to design peptides that exhibit chymotrypsin-like activity. Molecular modelling studies indicate that a 19-mer (chlida 2), which has a fRRM=0.2344 and φ=-1.186, folds appropriately so that the spatial separation of the amino acids required for chymotrypsin activity is comparable with that of α-chymotrypsin
  • Keywords
    molecular biophysics; organic compounds; physiological models; resonance; α-chymotrypsin-like peptides design; 19-mer; amino acids spatial separation; chlida 2; molecular modelling studies; resonant recognition model; Application specific processors; Australia; Biochemistry; Biological system modeling; Bovine; Frequency; Peptides; Sequences; Signal design; Signal to noise ratio;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Bioelectromagnetism, 1998. Proceedings of the 2nd International Conference on
  • Conference_Location
    Melbourne, Vic.
  • Print_ISBN
    0-7803-3867-7
  • Type

    conf

  • DOI
    10.1109/ICBEM.1998.666411
  • Filename
    666411
    • Link To Document
    https://search.isc.ac/dl/search/defaultta.aspx?DTC=49&DC=2232060