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Träfflista för sökning "WFRF:(Svensson Sven Erik) srt2:(2001-2004)"

Sökning: WFRF:(Svensson Sven Erik) > (2001-2004)

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  • Lind, Johan, et al. (författare)
  • Detection distance influencing escape behaviour in two parids (Parus major and P. caeruleus)
  • 2003
  • Ingår i: Journal of Avian Biology. - 0908-8857 .- 1600-048X. ; 34:3, s. 233-236
  • Tidskriftsartikel (refereegranskat)abstract
    • When birds are attacked by aerial predators they should benefit by adjusting their escape to the prevailing attack situation. One important factor likely to affect escape decisions of prey, to our knowledge not previously studied, is the distance at which the attacking predator is detected. We investigated if great tits Parus major and blue tits P. caeruleus alter their escape behaviour to two different detection distances (2.3 m and 1m) by simulating surprise attacks using a predator model. Both species used the information about detection distance when escaping by increasing the escape angle at the shorter detection distance. In addition, blue tits adjusted to the shorter detection distance by dodging sideways more frequently. Great tits escaped initially steeper and faster than blue tits, whereas blue tits increased escape angle and speed more than great tits along the measured distance after taking wing
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  • Svedhem, Sofia, et al. (författare)
  • Subtle differences in dissociation rates of interactions between destabilized human carbonic anhydrase II mutants and immobilized benzenesulfonamide inhibitors probed by a surface plasmon resonance biosensor
  • 2001
  • Ingår i: Analytical Biochemistry. - : Elsevier BV. - 0003-2697 .- 1096-0309. ; 296:2, s. 188-196
  • Tidskriftsartikel (refereegranskat)abstract
    • The development of commercial biosensors based on surface plasmon resonance has made possible careful characterization of biomolecular interactions. Here, a set of destabilized human carbonic anhydrase II (HCA II) mutants was investigated with respect to their interaction kinetics with two different immobilized benzenesulfonamide inhibitors. Point mutations were located distantly from the active site, and the destabilization energies were up to 23 kJ/mol. The dissociation rate of wild-type HCA II, as determined from the binding to the inhibitor with higher affinity, was 0.019 s−1. For the mutants, dissociation rates were faster (0.022–0.025 s−1), and a correlation between faster dissociation and a high degree of destabilization was observed. We interpreted these results in terms of increased dynamics of the tertiary structures of the mutants. This interpretation was supported by entropy determinations, showing that the entropy of the native structure significantly increased upon destabilization of the protein molecule. Our findings demonstrate the applicability of modern biosensor technology in the study of subtle details in molecular interaction mechanisms, such as the long-range effect of point mutations on interaction kinetics.
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