M F Lensink

Summary

Country: Belgium

Publications

  1. pmc Relating destabilizing regions to known functional sites in proteins
    Benoit H Dessailly
    Service de Conformation des Macromolécules Biologiques, Centre de Biologie Structurale et Bioinformatique, CP 263, Universite Libre de Bruxelles, Bruxelles, Belgium
    BMC Bioinformatics 8:141. 2007
  2. pmc Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase
    M F Lensink
    Department of Lipoprotein Chemistry, Faculty of Medicine and Health Sciences, Ghent, Belgium
    Biophys J 88:939-52. 2005
  3. ncbi request reprint Recognition-induced conformational changes in protein-protein docking
    M F Lensink
    Center for Structural Biology and Bioinformatics, Dept of Chemistry, Universite Libre De Bruxelles U L B, Boulevard de Triomphe CP 263, B 1050 Brussels, Belgium
    Curr Pharm Biotechnol 9:77-86. 2008
  4. ncbi request reprint Response of SCP-2L domain of human MFE-2 to ligand removal: binding site closure and burial of peroxisomal targeting signal
    M F Lensink
    Biocenter Oulu and Department of Biochemistry, University of Oulu, P O Box 3000, FIN 90014, Oulu, Finland
    J Mol Biol 323:99-113. 2002
  5. ncbi request reprint A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases
    A K Lappi
    Biocenter Oulu and Department of Biochemistry, University of Oulu, P O Box 3000, FIN 90014, Oulu, Finland
    J Mol Biol 335:283-95. 2004

Collaborators

  • Alain Prochiantz
  • Benoit H Dessailly
  • A K Lappi
  • Shoshana J Wodak
  • M Lobell
  • K E H Salo
  • H I Alanen
  • L W Ruddock
  • A H Juffer

Detail Information

Publications5

  1. pmc Relating destabilizing regions to known functional sites in proteins
    Benoit H Dessailly
    Service de Conformation des Macromolécules Biologiques, Centre de Biologie Structurale et Bioinformatique, CP 263, Universite Libre de Bruxelles, Bruxelles, Belgium
    BMC Bioinformatics 8:141. 2007
    ..In addition, to relate destabilizing regions to known functional sites, a novel benchmark consisting of a diverse set of hand-curated protein functional sites is derived...
  2. pmc Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase
    M F Lensink
    Department of Lipoprotein Chemistry, Faculty of Medicine and Health Sciences, Ghent, Belgium
    Biophys J 88:939-52. 2005
    ..Lipid disorder increases, through decreased order parameters of the lipids interacting with the penetratin side chains. Penetratin molecules at the membrane surface do not seem to aggregate...
  3. ncbi request reprint Recognition-induced conformational changes in protein-protein docking
    M F Lensink
    Center for Structural Biology and Bioinformatics, Dept of Chemistry, Universite Libre De Bruxelles U L B, Boulevard de Triomphe CP 263, B 1050 Brussels, Belgium
    Curr Pharm Biotechnol 9:77-86. 2008
    ..Here we present a survey of the existing computational techniques to model protein flexibility in the context of protein-protein docking...
  4. ncbi request reprint Response of SCP-2L domain of human MFE-2 to ligand removal: binding site closure and burial of peroxisomal targeting signal
    M F Lensink
    Biocenter Oulu and Department of Biochemistry, University of Oulu, P O Box 3000, FIN 90014, Oulu, Finland
    J Mol Biol 323:99-113. 2002
    ..The results are in accordance with plant nsLTPs, where a similar accommodation of binding pocket size was found after ligand binding/removal. Furthermore, the calculations support the suggestion of a ligand-assisted targeting mechanism...
  5. ncbi request reprint A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases
    A K Lappi
    Biocenter Oulu and Department of Biochemistry, University of Oulu, P O Box 3000, FIN 90014, Oulu, Finland
    J Mol Biol 335:283-95. 2004
    ..This intra-domain motion resolves the apparent dichotomy of the pK(a) requirements for the C-terminal active-site cysteine...