Water molecule contributions to proton spin–lattice relaxation in rotationally immobilized proteins

Goddard, Yanina A.; Korb, Jean-Pierre; Bryant, Robert G.

doi:10.1016/j.jmr.2009.04.001

Cited by 29 publications

(25 citation statements)

References 43 publications

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“…Their existence at temperatures well below 270 K indicates that a fraction of water, likely the tightly bound hydration layer, remains liquid well below normal freezing point of water. This is consistent with many studies that suggest that the hydration layer can remain mobile down to the temperatures of 240 K and below, depending on the techniques that are used to probe the motions . In the HP36 samples, the intensities of these HOD peaks are almost not visible at the lowest recorded temperature of about 250 K, with the exception of the sample labeled at the L75 position.…”

Section: Resultssupporting

confidence: 90%

“…This is consistent with many studies that suggest that the hydration layer can remain mobile down to the temperatures of 240 K and below, depending on the techniques that are used to probe the motions. [31][32][33] In the HP36 samples, the intensities of these HOD peaks are almost not visible at the lowest recorded temperature of about 250 K, with the exception of the sample labeled at the L75 position. Relatively higher amounts of liquid water linger for HP67 at subfreezing temperatures.…”

Section: Vugmeyster Et Almentioning

confidence: 93%

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Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein

Vugmeyster

Ostrovsky

et al. 2013

Protein Science

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Thermostable villin headpiece protein (HP67) consists of the N-terminal subdomain (residues 10-41) and the autonomously folding C-terminal subdomain (residues 42-76) which pack against each other to form a structure with a unified hydrophobic core. The X-ray structures of the isolated C-terminal subdomain (HP36) and its counterpart in HP67 are very similar for the hydrophobic core residues. However, fine rearrangements of the free energy landscape are expected to occur because of the interactions between the two subdomains. We detect and characterize these changes by comparing the ms-ms time scale dynamics of the methyl-bearing side chains in isolated HP36 and in HP67. Specifically, we probe three hydrophobic side chains at the interface of the two subdomains (L42, V50, and L75) as well as at two residues far from the interface (L61 and L69). Solid-state deuteron NMR techniques are combined with computational modeling for the detailed characterization of motional modes in terms of their kinetic and thermodynamic parameters. The effect of interdomain interactions on side chain dynamics is seen for all residues but L75. Thus, changes in dynamics because of subdomain interactions are not confined to the site of perturbation. One of the main results is a two-to threefold increase in the value of the activation energies for the rotameric mode of motions in HP67 compared with HP36. Detailed analysis of configurational entropies and heat capacities complement the kinetic view of the degree of the disorder in the folded state.

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Section: Resultssupporting

confidence: 90%

Section: Vugmeyster Et Almentioning

confidence: 93%

Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein

Vugmeyster

Ostrovsky

et al. 2013

Protein Science

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“…Correlation times τ obtained from R 1ρ dispersion profiles, are comparable with results obtained using other methods for investigations of molecular motion in proteins [1,3,6]. We found that these correlation times for proteins are not strongly dependent on hydration level (see Table II and Fig.…”

Section: Resultssupporting

confidence: 87%

“…One of these methods is nuclear magnetic relaxation dispersion [1][2][3][4][5][6][7], that is the measurement of nuclear magnetic relaxation rates R i = 1/T i (i = 1, 2, 1ρ) as a function of the magnetic field strength. In particular, there are some of interesting publications on molecular dynamics of proteins based on the spin-lattice relaxation rate, R 1 , dependence on B 0 [1][2][3][4][5] and the spin-lattice relaxation rate in the rotating frame, R 1ρ , dependence on B 1 [6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Molecular Dynamics in Biological Systems Observed by NMR Relaxation in a Rotating Frame

2012

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NMR relaxation provides powerful tools for obtaining information on three-dimensional structures, dynamic properties and intermolecular interactions of biological macromolecules. One of these methods, called dispersion profile, is based on measuring the field dependence of spin-relaxation rates in the rotating frame, R1ρ = 1/T1ρ, in the presence of a low magnetic field B1. In the presented study we use this method for investigation of molecular dynamics in protein samples. Dispersion profiles can be predicted theoretically and using two models, assuming either dipolar interaction between protons or power law dispersion, we have evaluated some molecular dynamic parameters of water adsorbed on protein surface. Our researches are focused on the connections of obtained parameters of molecular dynamics with conformation changes of protein. We have calculated the correlation times and power parameters for samples of lyophilized powder of albumins (egg white and bovine and rabbit blood serum) and lysozyme, as well as its aqueous solutions. Analysis of these parameters yields valuable information on the molecular nature of investigated biological systems. We also used this method to analyze experimental data of T1ρ obtained by other authors for bovine serum albumin and we have found good accordance with their conclusions concerning molecular dynamics of proteins.

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“…Some representative examples of the problems addressed by researchers are fluid dynamics at the solid interface, transport in porous media (filtration, imbibition, and conduction), [21] role of physical chemistry at the pore surface (proton exchange and wettability), [22,23] phase transitions in confinement, hydration of proteins, biological tissues and membranes, [24][25][26][27][28] dynamics of water at the protein surface, [29][30][31][32][33][34][35] dynamics of polymers [36][37][38][39][40][41] and liquid crystals, [12,[42][43][44][45] and the study of MRI contrast agents and differential diagnosis.…”

Section: Discussionmentioning

confidence: 99%

New applications and perspectives of fast field cycling NMR relaxometry

Steele

Korb

Ferrante

et al. 2015

Magnetic Reson in Chemistry

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The field cycling NMR relaxometry method (also known as fast field cycling (FFC) when instruments employing fast electrical switching of the magnetic field are used) allows determination of the spin-lattice relaxation time (T1 ) continuously over five decades of Larmor frequency. The method can be exploited to observe the T1 frequency dependence of protons, as well as any other NMR-sensitive nuclei, such as (2) H, (13) C, (31) P, and (19) F in a wide range of substances and materials. The information obtained is directly correlated with the physical/chemical properties of the compound and can be represented as a 'nuclear magnetic resonance dispersion' curve. We present some recent academic and industrial applications showing the relevance of exploiting FFC NMR relaxometry in complex materials to study the molecular dynamics or, simply, for fingerprinting or quality control purposes. The basic nuclear magnetic resonance dispersion features are outlined in representative examples of magnetic resonance imaging (MRI) contrast agents, porous media, proteins, and food stuffs. We will focus on the new directions and perspectives for the FFC technique. For instance, the introduction of the latest Wide Bore FFC NMR relaxometers allows probing, for the first time, of the dynamics of confined surface water contained in the macro-pores of carbonate rock cores. We also evidence the use of the latest field cycling technology with a new cryogen-free variable-field electromagnet, which enhances the range of available frequencies in the 2D T1 -T2 correlation spectrum for separating oil and water in crude oil. Copyright © 2015 John Wiley & Sons, Ltd.

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Water molecule contributions to proton spin–lattice relaxation in rotationally immobilized proteins

Cited by 29 publications

References 43 publications

Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein

Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein

Molecular Dynamics in Biological Systems Observed by NMR Relaxation in a Rotating Frame

New applications and perspectives of fast field cycling NMR relaxometry

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