Mean-squared atomic displacements in hydrated lysozyme, native and denatured

Mamontov, Eugene; O’Neill, Hugh; Zhang, Qiu

doi:10.1007/s10867-009-9184-6

Cited by 44 publications

(36 citation statements)

References 51 publications

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“…For example, J. Pieper et al, in the case of hydrated Photosystem (PS) II, have demonstrated that the PDT occurs at the same temperature value at which the electron transport efficiency highly increases [12]; however, several exceptions exist [13][14][15]: e.g. in Ref.…”

mentioning

confidence: 99%

RETRACTED: Protein dynamics by neutron scattering

Benedetto

2013

Biophysical Chemistry

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mentioning

confidence: 99%

RETRACTED: Protein dynamics by neutron scattering

Benedetto

2013

Biophysical Chemistry

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“…Thus, we can expect that is also the same whether the biomolecule is native or denatured. This expectation is in accord with the results of elastic neutron scattering experiment by Mamontov et al [67] Before one can take these deviations seriously one should be mindful of the large error involved in determining dielectric relaxation data at high frequencies near 1 GHz (the upper limit of the frequency range of the spectrometer used), but the errors were not reported by the authors of [25].…”

Section: Same Dynamics Transition and T D In Both Hydrated Native Andsupporting

confidence: 82%

Resolving the ambiguity of the dynamics of water and clarifying its role in hydrated proteins

Ngai

Capaccioli

Ancherbak

et al. 2011

Philosophical Magazine

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The dynamics of water in aqueous mixtures with various hydrophilic solutes can be probed over practically unrestricted temperature and frequency ranges, in contrast to bulk water where crystallization preempts such study. The characteristics of the dynamics of water and their trends observed in aqueous mixtures on varying the solutes and concentration of water, in conjunction with that of water confined in spaces of nanometer size, lead us to infer the fundamental traits of the dynamics of water. These include the universal secondary relaxation, here called the nu-relaxation, the low degree of intermolecular coupling/cooperativity, and the 'strong' character of the structural primary relaxation. The dynamics of hydration water in hydrated proteins at sufficiently high hydration levels are similar in every respect to that in aqueous mixtures. In particular, the nu-relaxation of hydration water has a relaxation time nearly the same as that of the nu-relaxation of aqueous mixtures above and below the glass transition temperature. This can explain the dynamics transition observed by Mossbauer spectroscopy and neutron scattering. The fact that it is coupled to atomic motions of the hydrated protein, like similar situation in aqueous mixtures, explains why the dynamic transition is observed by neutron scattering at the same temperature whether the hydration water is H(2)O or D(2)O. The possibility that the nu-relaxation of the solvent is instrumental for biological function of hydrated biomolecules is suggested by the comparable temperature dependences of the ligand escape rate and the reciprocal of the nu-relaxation time

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“…It should also be noted that in the nanosecond time scale used in the mentioned studies a significant contribution to the MSD of protein powders comes from methyl group rotations, and it masks changes in MSD that may result from unfolding. 26 We also remark that the degree of folding and exposure to water can vary significantly among different IDPs and proteins of varied unfolded content. 4 Consequently, the dynamical and mechanical properties of such proteins, as well as the coupling between protein and hydration water motions, 14 can change as a function of the compactness of the conformation.…”

Section: ■ Introductionmentioning

confidence: 79%

Dynamics and Rigidity in an Intrinsically Disordered Protein, β-Casein

et al. 2014

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The emergence of intrinsically disordered proteins (IDPs) as a recognized structural class has forced the community to confront a new paradigm of structure, dynamics, and mechanical properties for proteins. We present novel data on the similarities and differences in the dynamics and nanomechanical properties of IDPs and other biomacromolecules on the picosecond time scale. An IDP, β-casein (CAS), has been studied in a calcium bound and unbound state using neutron and light scattering techniques. We show that CAS partially folds and stiffens upon calcium binding, but in the unfolded state, it is softer than folded proteins such as green fluorescence protein (GFP). We also see that some localized diffusive motions in CAS have a larger amplitude than in GFP at this time scale but are still smaller than those observed in tRNA. In spite of these differences, CAS dynamics are consistent with the classes of motions seen in folded protein on this time scale.

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Mean-squared atomic displacements in hydrated lysozyme, native and denatured

Cited by 44 publications

References 51 publications

RETRACTED: Protein dynamics by neutron scattering

RETRACTED: Protein dynamics by neutron scattering

Resolving the ambiguity of the dynamics of water and clarifying its role in hydrated proteins

Dynamics and Rigidity in an Intrinsically Disordered Protein, β-Casein

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