Showing papers by "Chris Sander published in 1985"
TL;DR: A new method for modelling protein dynamics using normal-mode analysis in internal co-ordinates, particularly well suited for modelling collective motion, makes possible direct visualization of biologically interesting modes, and is complementary to the more time-consuming simulation of molecular dynamics trajectories.
702 citations
TL;DR: Analysis of the amino acid sequence of transcription factor TFIIIA from Xenopuslaevis reveals the presence of 12 repeating structures, each about 30 residues in length, which may be used to coordinate a zinc cation.
347 citations
17 citations
TL;DR: The normal mode dynamics of the enzymes lysozyme and ribonuclease are calculated and it is shown that jawlike behaviour is due to the collective motion of entire protein domains and is likely to facilitate catalysis.
Abstract: Offprint requests to C Sander dominate atomic displacements and that surprisingly few of these suffice to describe experimentally determined fluctuations of atomic position We have now calculated the normal mode dynamics of the enzymes lysozyme and ribonuclease [2] A film of their lowest frequency normal modes shows opening and closing of the active site cleft This jawlike behaviour is due to the collective motion of entire protein domains and is likely to facilitate catalysis We are led to the suggestion that optimization of enzyme function in natural evolution or genetic engineering must affect not only the nature and positioning of active site residues but also the nature and positioning of key residues modulating domain dynamics
1 citations