Journal ArticleDOI
Nanosecond Fluorescence Dynamic Stokes Shift of Tryptophan in a Protein Matrix
Michel Vincent,‡ Anne-Marie Gilles,Ines M. Li De La Sierra,Pierre Briozzo,and Octavian Bârzu,Jacques Gallay +5 more
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TLDR
A time constant affected by a negative preexponential, evidenced in the red-edge fluorescence intensity decays, supports the existence of an excited-state reaction.Abstract:
The fluorescent dynamic Stokes shift (FDSS) method has emphasized a time-dependent dipolar relaxation process around the single tryptophan residue (Trp31) in cytidine monophosphate kinase from E. coli (CMPK). This Trp residue, located close to the protein surface in a hydrophobic pocket, is weakly accessible to acrylamide, a water-soluble quencher. It exhibits fluorescence characteristics suitable for a detailed study of dipolar relaxation: (i) a fluorescence decay almost monoexponential and (ii) a fluorescence emission maximum of 329 nm, in a wavelength range intermediate between those of a completely polar environment and a strongly apolar one. This emission maximum is shifted to 320 nm by decreasing the temperature to 230−240 K with glycerol as cryoprotectant. A time constant (∼100 ps) affected by a negative preexponential, evidenced in the red-edge fluorescence intensity decays, supports the existence of an excited-state reaction. A multiphasic FDSS (with time constants ranging from ∼100 ps to severa...read more
Citations
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Biological water at the protein surface: dynamical solvation probed directly with femtosecond resolution.
TL;DR: Results show that hydration at the surface is a dynamical process with two general types of trajectories, those that result from weak interactions with the selected surface site, giving rise to bulk-type solvation, and those that have a stronger interaction, enough to define a rigid water structure, with a solvation time of 38 ps, much slower than that of the bulk.
Journal ArticleDOI
The red‐edge effects: 30 years of exploration
TL;DR: Red-edge effects were discovered for electron-transfer and proton-transfer reactions if they depended on the dynamics of the environment and stimulated the emergence and development of cryogenic energy-selective and single-molecular techniques that became valuable tools in their own right in chemistry and biophysics research.
Journal ArticleDOI
Electrostatics and dynamics of proteins
TL;DR: In this paper, a simple framework to rationalize the results is continuum electrostatics, even though proteins are smaller than the usual, macroscopic length scales of continuum theory, and the physical and numerical basis of current continuum models of proteins and protein solvation.
Journal ArticleDOI
Dynamic Stokes shift in green fluorescent protein variants
TL;DR: The evolutionary pathway and structures of related fluorescent proteins suggest the role of a single residue in close proximity to the chromophore as the primary cause of the solvation response, which is absent in wild-type green fluorescent protein.
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Quantum dynamics of electronic excitations in biomolecular chromophores: role of the protein environment and solvent
Joel Gilmore,Ross H. McKenzie +1 more
TL;DR: In this article, the spectral density of a biomolecular chromophore was derived for a wide range of proteins, proteins, and solvents, and the results provided a natural description of the different time scales observed in ultrafast laser spectroscopy, including three pulse photon echo decay and dynamic Stokes shift measurements.
References
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Journal ArticleDOI
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
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Subpicosecond Measurements of Polar Solvation Dynamics: Coumarin 153 Revisited
TL;DR: In this article, the authors used time-resolved emission measurements of the solute coumarin 153 (C153) to probe the time dependence of solvation in 24 common solvents at room temperature.
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Picosecond solvation dynamics of coumarin 153: The importance of molecular aspects of solvation
TL;DR: In this paper, a probe molecule coumarin 153 (Cu153) and picosecond spectroscopic techniques were used to examine the solvation dynamics in polar liquids and showed that the frequency of the electronic spectrum of this probe provides a convenient measure of solvation energetics.
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Temperature-dependent X-ray diffraction as a probe of protein structural dynamics
Hans Frauenfelder,Hans Frauenfelder,Gregory A. Petsko,Gregory A. Petsko,Gregory A. Petsko,Demetrius Tsernoglou,Demetrius Tsernoglou +6 more
TL;DR: It is concluded that X-ray diffraction can provide the spatial distribution of the dynamic features of a protein.
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Dynamical transition of myoglobin revealed by inelastic neutron scattering.
TL;DR: The dynamical behaviour of myoglobin (and other globular proteins) suggests a coupling of fast local motions to slower collective motions, which is a characteristic feature of other dense glass-forming systems.