2011
DOI: 10.1021/bi200206z
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Light-Controlled Protein Dynamics Observed with Neutron Spin Echo Measurements

Abstract: A photoresponsive surfactant has been used as a means to control protein structure and dynamics with light illumination. This cationic azobenzene surfactant, azoTAB, which undergoes a reversible photoisomerization upon exposure to the appropriate wavelength of light, adopts a relatively hydrophobic, trans structure under visible light illumination and a relatively hydrophilic cis structure under UV light illumination. Small-angle neutron scattering (SANS) and neutron spin echo (NSE) spectroscopy were used to m… Show more

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Cited by 12 publications
(14 citation statements)
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“…WAXS data reinforces the coherent S coh ( q , t ) interdomain NSE results quite precisely. This principle of de Gennes narrowing for interdomain motion has been demonstrated for several proteins recently . In our case too, the wave vector dependence of the interdomain diffusion coefficient is inversely proportional to the interdomain structure factor.…”
Section: Resultsmentioning
confidence: 92%
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“…WAXS data reinforces the coherent S coh ( q , t ) interdomain NSE results quite precisely. This principle of de Gennes narrowing for interdomain motion has been demonstrated for several proteins recently . In our case too, the wave vector dependence of the interdomain diffusion coefficient is inversely proportional to the interdomain structure factor.…”
Section: Resultsmentioning
confidence: 92%
“…Neutron spin‐echo spectroscopy (NSE) is a probe of protein dynamics sensitive to slow correlated motions (including translational and rotational diffusion and internal modes) on the picosecond to nanosecond time scale. NSE provides information about the time evolution of structural correlations analogous to dynamic light scattering but at time and length scales more relevant to protein internal modes . Recent NSE studies of Hb and myoglobin (Mb) utilized data up to a very high momentum transfer q (∼0.62 Å −1 ) to characterize the internal dynamics of these proteins in terms of the dynamic pair correlation function and self‐correlation function in the time range of several picoseconds to a few nanoseconds.…”
Section: Introductionmentioning
confidence: 99%
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“…In the case of carbonic anhydrase, for example, the protein was found to dramatically unfold and, thus, inactivate in the presence of the trans surfactant, while the unfolding was reversed to a native‐like enzyme conformation and activity upon UV illumination, resulting in enzyme reactivation . In contrast, lysozyme in the presence of the trans isomer was found to exhibit eightfold superactivity (ie, activity greater than the native enzyme), a result of enhanced enzyme flexibility as indicated through an increase in nanosecond domain motions . In addition, azoTAB has been shown to primarily interact with helical regions within proteins that are generally hydrophobic, as observed for bovine serum albumin where azoTAB‐induced unfolding was initially restricted to α‐helical segments in the C‐terminal part of the molecule .…”
Section: Introductionmentioning
confidence: 99%
“…What transpired as a consequence, was a case of cis‐trans isomerization.Such photo‐isomerization of azo benzenes is important for several biological processes with implications in pharmacology and cell biology. Hence, we decided to pursue the matter further for it might play an important role if the compound had anti‐microbial activity …”
Section: Introductionmentioning
confidence: 99%