Proteases and protein stability

  • Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface; A. Bjørk, B. Dalhus, D. Mantzilas, R. Sirevåg, V.G.H. Eijsink, J. Mol. Biol. 341 (2004) 1215-1226. pdf
  • The Effects of Modifying the Surface Charge on the Catalytic Activity of a Thermolysin-like Protease. Arno de Kreij, Bertus van den Burg, Gerard Venema, Gert Vriend,Vincent G. H. Eijsink and Jens E. Nielsen. The Journal of Biological Chemistry. 277 (2002) 15432–15438. pdf
  • The effect of changing the hydrophobic S1' subsite of thermolysin-like proteases on substrate specificity.de Kreij, Arno, van den Burg, Bertus, Veltman, Oene R., Vriend, Gert, Venema, Gerard, Eijsink, Vincent G. H. Eur J Biochem. 268 (2001) 4985-4991. pdf
  • Engineering a hyperstable enzyme by manipulation of early steps in the unfolding process; V.G.H. Eijsink, G. Vriend, B. van den Burg; Biocatalysis and Biotransformation, 19 (2001) 443-458. pdf
  • Probing the unfolding region in thermolysin-like proteases by site-specific immobilization; J. Mansfeld, G. Vriend, B. van den Burg, V.G.H. Eijsink, R. Ulbrich-Hofmann; Biochemistry 38 (1999) 8240-8245. pdf
  • Engineering an enzyme to resist boiling; B. van den Burg, G. Vriend, O.R. Veltman, G. Venema, V.G.H. Eijsink; Proc. Natl. Acad. Sci. USA, 95 (1998) 2056-2060. pdf
  • Rendering one autolysis site in Bacillus subtilis neutral protease resistant to cleavage reveals a new fission; B. van den Burg, V.G.H. Eijsink, G. Vriend, O.R. Veltman, G. Venema; Biotechnol. Appl. Biochem. 27 (1998) 125-132. pdf
  • A single calcium binding site is crucial for the calcium dependent thermal stability of thermolysin-like proteases; O. R. Veltman, G. Vriend, H.J.C. Berendsen, B. van den Burg, G. Venema, V.G.H. Eijsink; Biochemistry 37 (1998) 5312-5319. pdf
  • Probing possible catalytic hinge bending motions in thermolysin-like proteases by Gly -> Ala mutations; O.R. Veltman, V.G.H. Eijsink, G. Vriend, A. De Kreij, G. Venema, B. van den Burg; Biochemistry 37 (1998) 5305-5311. pdf
  • Early steps in the unfolding of thermolysin-like proteases; G. Vriend, H.J.C. Berendsen, B. van den Burg, G. Venema, V.G.H. Eijsink; J. Biol. Chem. 273 (1998) 35074-35077. pdf
  • Model building of a thermolysin-like protease by mutagenesis; F. Frigerio, I. Margarit, R. Nogarotto, G. Grandi, G. Vriend, F. Hardy, G. Venema, V.G.H. Eijsink; Protein Engng. 10 (1997) 223-230. pdf
  • Manipulating the autolytic pathway of a Bacillus protease; B. van den Burg, V.G.H. Eijsink, G. Vriend, O.R. Veltman, G. Venema; In: Proteolysis in Cell Function (V.K. Hopsu-Havu, M. Järvinen, H. Kirschke, eds.), IOS Press, The Netherlands, 1997, pp. 120-127.
  • Engineering thermolysin-like proteases whose stability is largely independent of calcium; O.R. Veltman, G. Vriend, B. van den Burg, F. Hardy, G. Venema, V.G.H. Eijsink; FEBS letters 405 (1997) 241-244. pdf
  • Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond; J. Mansfeld, G. Vriend, B.W. Dijkstra, O.R. Veltman, B. van den Burg, G. Venema, R. Ulbrich-Hofman, V.G.H. Eijsink; J. Biol. Chem. 272 (1997) 11152-11156. pdf
  • Mutational analysis of a surface area that is critical for the thermal stability of thermolysin-like proteases; O.R. Veltman, G. Vriend, F. Hardy, J. Mansfeld, B. van den Burg, G. Venema, V.G.H. Eijsink; Eur. J. Biochem. 248 (1997) 433-440. pdf
  • Analysis of the structural determinants of the stability of thermolysin-like proteases by molecular modelling and site-directed mutagenesis; O.R. Veltman, G. Vriend, P.J. Middelhoven, B. van den Burg, G. Venema, V.G.H. Eijsink; Protein Engng. 9 (1996) 1181-1189. pdf
  • Structural determinants of the thermostability of thermolysin-like proteases; V.G.H. Eijsink, O.R. Veltman, W. Aukema, G. Vriend, G. Venema; Nature Struct. Biol. 2 (1995) 374-379
  • The essential dynamics of thermolysin - confirmation of the hinge-bending motion and comparison of simulations in vacuum and water; D.M.F. van Aalten, A. Amadei, A.B.M. Linssen, V.G.H. Eijsink, G. Vriend, H.J.C. Berendsen; Proteins 22 (1995) 45-54