Dynamics of metmyoglobin crystals investigated by nuclear gamma resonance absorption

Parak, F.; Frolov, E. N.; Mößbauer, R. L.; Goldanskii, V. I.

doi:10.1016/0022-2836(81)90317-x

Cited by 234 publications

(129 citation statements)

References 21 publications

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“…These measurements were again performed on the enzyme xylanase at different CD 3 The measured transmissions (and respective protein concentrations) were 0.92 (76 mg ml À1 ), 0.92 (88 mg ml À1 ), 0.95 (71 mg ml À1 ), 0.94 (71 mg ml À1 ) and 0.97 (66 mg ml À1 ), respectively. Samples were cooled to 80 K then heated progressively to 320 K over 22 h, during which time the data were collected.…”

Section: Data Collectionmentioning

confidence: 99%

“…Experimental techniques such as Mo¨ssbauer spectroscopy, X-ray diffraction and neutron scattering have suggested the presence of a transition in the internal dynamics of protein motions at B180-220 K. [1][2][3][4][5][6][7][8][9] This apparent dynamical transition has been observed to have similarities to the phase transition that appears in glass-forming liquids. [10][11][12][13] The motions below the transition are believed to be mostly harmonic whereas the mean-square displacements above the transition are dominated by anharmonic contributions.…”

Section: Introductionmentioning

confidence: 99%

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Temperature and timescale dependence of protein dynamics in methanol : water mixtures

Tournier

Réat

Dunn

et al. 2005

Phys. Chem. Chem. Phys.

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Experimental and computer simulation studies have suggested the presence of a transition in the dynamics of hydrated proteins at around 180-220 K. This transition is manifested by nonlinear behaviour in the temperature dependence of the average atomic mean-square displacement which increases at high temperature. Here, we present results of a dynamic neutron scattering analysis of the transition for a simple enzyme: xylanase in water : methanol solutions of varying methanol concentrations. In order to investigate motions on different timescales, two different instruments were used: one sensitive to B100 ps timescale motions and the other to Bns timescale motions. The results reveal distinctly different behaviour on the two timescales examined. On the shorter timescale the dynamics are dictated by the properties of the surrounding solvent: the temperature of the dynamical transition lowers with increasing methanol concentration closely following the melting behaviour of the corresponding water : methanol solution. This contrasts with the longer (ns) timescale results in which the dynamical transition appears at temperatures lower than the corresponding melting point of the cryosolvent. These results are suggested to arise from a collaborative effect between the protein surface and the solvent which lowers the effective melting temperature of the protein hydration layer. Taken together, the results suggest that the protein solvation shell may play a major role in the temperature dependence of protein solution dynamics.

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Section: Data Collectionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Temperature and timescale dependence of protein dynamics in methanol : water mixtures

Tournier

Réat

Dunn

et al. 2005

Phys. Chem. Chem. Phys.

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show abstract

“…A variety of experiments have demonstrated the existence of a dynamical transition in hydrated proteins at ca. 180-220 K, characterized by deviation from linearity of the temperature dependence of the mean-square displacement, ͗u 2 ͘ (Cohen et al 1981;Parak et al 1981;Knapp et al 1982;Doster et al 1989Doster et al , 1990Rasmussen et al 1992;Tilton et al 1992;Ferrand et al 1993;Green et al 1994;Fitter et al 1997;Daniel et al 1998Daniel et al , 1999Reat et al 2000;Bicout & Zaccai 2001;Lee & Wand 2001;Teeter et al 2001). The protein transition has dynamical aspects in common with the liquid-glass transition.…”

Section: Solvent Role In the Protein-glass Transitionmentioning

confidence: 99%

Structure, dynamics and reactions of protein hydration water

Smith

Merzel

Bondar

et al. 2004

Phil. Trans. R. Soc. Lond. B

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The apparent simplicity of the water molecule belies the wide range of fascinating protein phenomena in which it participates. We review recent computer simulation work on buried, internal water molecules, discussing the thermodynamics of water molecule binding and the participation of water in proton transfer reactions. Surface water molecules are also considered, with emphasis on the modification of average solvent structure on a protein surface, the role of water in the protein dynamical 'glass' transition and a simplified description of the protein motions thereby activated.

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“…These include Mö ssbauer spectroscopy of the Fe ion in myoglobin, X-ray scattering measurements of the temperature factor in protein crystals, Rayleigh scattering of Mö ssbauer radiation, and neutron scattering to probe the global dynamics of a relatively limited number of proteins. [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16] Depending on the technique and possibly the protein or the nature of the preparation, the sharpness and temperature of this transition may vary somewhat, but has been generally observed between about 180 and 230 K. It is taken to be an intrinsic property of proteins and, as indicated above, has been associated with the onset of protein function. [14][15][16][17][18][19][20] Recent neutron scattering measurements on a thermophilic glutamate dehydrogenase enzyme in solution, under conditions in which enzyme activity is both possible and measurable, failed to show any relationship between an observed dynamical transition at around 220 K and the onset of activity 13 (Fig.…”

Section: Introductionmentioning

confidence: 99%

The dynamic transition in proteins may have a simple explanation

2002

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The transition that has been observed in the dynamics of hydrated proteins at low temperatures (180-230 K) is normally interpreted as a change from vibrational, harmonic motion at low temperatures to anharmonic motions as the temperature is raised. It is taken to be an intrinsic property of proteins and has been associated with the onset of protein functions. Examination of the dynamic behaviour of proteins in solution within a defined timescale window suggests that certain observations can be explained without the need to invoke a discontinuity in the dynamics of proteins with temperature, i.e. the existence of a dynamical transition is not required. This is discussed in the context of recent evidence that enzyme activity is independent of the activation of anharmonic picosecond dynamics and declines steadily with temperature through the apparent dynamic transition, in accordance with the Arrhenius relationship. That similar timescale dependent dynamical behaviour has been observed experimentally in chain polymers, and seen also in computer simulations of silica glasses, suggests that the phenomenon may be of wide general relevance in both simple glassy and more complex polymeric systems.

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Dynamics of metmyoglobin crystals investigated by nuclear gamma resonance absorption

Cited by 234 publications

References 21 publications

Temperature and timescale dependence of protein dynamics in methanol : water mixtures

Temperature and timescale dependence of protein dynamics in methanol : water mixtures

Structure, dynamics and reactions of protein hydration water

The dynamic transition in proteins may have a simple explanation

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