2012
DOI: 10.1002/iub.1101
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Internal friction in enzyme reactions

Abstract: The empirical concept of internal friction was introduced 20 years ago. This review summarizes the results of experimental and theoretical studies that help to uncover the nature of internal friction. After the history of the concept, we describe the experimental challenges in measuring and interpreting internal friction based on the viscosity dependence of enzyme reactions. We also present speculations about the structural background of this viscosity dependence. Finally, some models about the relationship be… Show more

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Cited by 15 publications
(19 citation statements)
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“…We detect a significant trend towards more of the latter, 519 for instance in the use 368,1235,1296,1297 of molecular dynamics to calculate properties that suggest which residues might be creating internal friction 1298,1299 and hence lowering k cat . These examples help to illustrate that predictions and simulations in silico are likely to play an increasingly important role in predicting strategies for mutagenesis in vitro .…”
Section: Concluding Remarks and Future Prospectsmentioning
confidence: 83%
“…We detect a significant trend towards more of the latter, 519 for instance in the use 368,1235,1296,1297 of molecular dynamics to calculate properties that suggest which residues might be creating internal friction 1298,1299 and hence lowering k cat . These examples help to illustrate that predictions and simulations in silico are likely to play an increasingly important role in predicting strategies for mutagenesis in vitro .…”
Section: Concluding Remarks and Future Prospectsmentioning
confidence: 83%
“…The Stokes–Einstein relationship predicts a β of unity and therefore a linear dependence of rate on viscosity, but β values between 0 and 1 and even deviations from linearity have been observed. 54 Tollinger et al demonstrated a linear decrease of the SH3 folding rate with increasing viscosity in glycerol. 55 Therefore, we assumed a β of unity for the small cosolutes and adjusted the folding rates accordingly ko=kηnormalcηbuffer,303K=kηrel where k 0 is the viscosity-adjusted rate, η c is the viscosity, η buffer,303K is the viscosity of water at 303 K (0.8 cP), and η rel is the viscosity adjusted to buffer at 303 K. Wong et al 25 and Perl et al 27 used similar analyses.…”
Section: Resultsmentioning
confidence: 99%
“…Taking a rest length ℓ 0 ≃ 5 nm and internal viscosity of η ≃ 10 −2 Pa s [99,100], we obtain the friction coefficient, γ ≃ 3πηℓ 0 ≃ 10 −10 kg/s, which sets the thermal timescale τ 0 = γ/a ≃ 1 µs with a = 0.1 pN/nm. Now we compute the reaction rate for our test enzyme over a range of σ A and τ A for two different energy barriers, E B = 6 k B T (Fig.…”
Section: Resultsmentioning
confidence: 99%