Hydration dependence of backbone and side chain polylysine dynamics: A <sup>13</sup>C solid‐state NMR and IR spectroscopy study

Krushelnitsky, Alexey; Faizullin, Dzhigangir A.; Reichert, Detlef

doi:10.1002/bip.10540

Cited by 18 publications

(53 citation statements)

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“…Hydration of initially dry protein powders results in increasing amplitude and decreasing correlation time of slow motion, at the same time hardly affecting faster motions. Unlike previously studied lysozyme, binase and bovine albumin [7][8][9][10], the human albumin displayed a stronger dependence of relaxation on hydration. Here, we present a detailed investigation of human albumin in wateracetonitrile mixtures and compare them with our previous results, obtained on the same protein hydrated by pure water.…”

Section: Introductionmentioning

confidence: 72%

“…In polypeptides having no methyl groups in their chemical structure and also in isotopically labeled proteins the third transition was clearly detected in the temperature region between 110 and 160 K [4,[8][9][10]. It has been referred to fast oscillations of side chain groups.…”

Section: Relationship Of Nmr Measurements To Mobilitymentioning

confidence: 90%

“…2, two minima on the temperature dependences of T~ are clearly observed for all HSA samples. The low-temperature minimum at 160 K arises from the high-frequency methyl rotation [5,6] and the high-temperature minimum originates from the slow side chain motion [7][8][9][10]. The shifting of the T 1 minimum downward on the temperature scale could result for several reasons including changes of the activation energy, correlation times or the amplitude of the group oscillations.…”

Section: Relationship Of Nmr Measurements To Mobilitymentioning

confidence: 99%

“…To proceed from NMR relaxation times to the true microdynamic parameters, it is necessary to carry out measurements in temperature range as wide as, possible (100--400 K) and at multiple resonance frequencies [5,6]. Here we analyzed relaxation times by the correlation function formalism on the basis of the model-free approach that we used before [4,[6][7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

“…Upon studying solid proteins and polypeptides, we have revealed three different internal motions covering the time scale from hundreds of picoseconds to microseconds [7][8][9][10]. It has been shown that the slowest motion is strongly enhanced on hydration.…”

Section: Introductionmentioning

confidence: 99%

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Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by1H NMR relaxation and FTIR spectroscopy

2005

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Abstraer. The effect of acetonitrile on protein dynamics was investigated for solid human serum albumin samples at various hydration levels. Temperature dependences of ~H nonselective nuclear magnetic resonance T~ and T2 relaxation times at 27 MHz have been measured and data were interpreted in terms of three kinds of internal motions in the protein. Microdynamic parameters of the motions were obtained within a "model-free" approach. It was found that acetonitrile hardly affects the fast motions but noticeably influences the slow motion of side chain groups, shortening the cor~elation time and increasing the amplitude of the motion. The acetonitrile effect on dynamics is likely based on the appearance of additional free volume asa result of the formation of ¡ helical parts in the protein structure. Water, plasticizing the protein structure, promotes the action of organic solvent. A definite part of side chain groups, slowly moving in the same frequency window as the rest of protein side chain groups, performs less constrained "liquidlike" motion. The relative population of these highly movable protons is closely correlated with the increment of the helical structure induced by water and acetonitrile.

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Section: Introductionmentioning

confidence: 72%

Section: Relationship Of Nmr Measurements To Mobilitymentioning

confidence: 90%

Section: Relationship Of Nmr Measurements To Mobilitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by1H NMR relaxation and FTIR spectroscopy

2005

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Complex ¹H,¹³C‐NMR relaxation and computer simulation study of side‐chain dynamics in solid polylysine

Krushelnitsky

Reichert²

2005

Biopolymers

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The side-chain dynamics of solid polylysine at various hydration levels was studied by means of proton spin-lattice relaxation times measurements in the laboratory and tilted (off-resonance) rotating frames at several temperatures as well as Monte Carlo computer simulations. These data were analyzed together with recently measured carbon relaxation data (A. Krushelnitsky, D. Faizullin, and D. Reichert, Biopolymers, 2004, Vol. 73, pp. 1-15). The analysis of the whole set of data performed within the frame of the model-free approach led us to a conclusion about three types of the side-chain motion. The first motion consists of low amplitude rotations of dihedral angles of polylysine side chains on the nanosecond timescale. The second motion is cis-trans conformational transitions of the side chains with correlation times in the microsecond range for dry polylysine. The third motion is a diffusion of dilating defects described in (W. Nusser, R. Kimmich, and F. Winter, Journal of Physical Chemistry, 1988, Vol. 92, pp. 6808-6814). This diffusion causes almost no reorientation of chemical bonds but leads to a sliding motion of side chains with respect to each other in the nanosecond timescale. This work evidently demonstrates the advantages of the simultaneous quantitative analysis of data obtained from different experiments within the frame of the same mathematical formalism, providing for the detailed description of the nature and geometry of the internal molecular dynamics.

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Response of lysozyme internal dynamics to hydration probed by13C and1H solid-state NMR relaxation

2004

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We have studied the hydration dependence of the internal protein dynamics of hen egg white lysozyme by naturally abundant ~3C and ~H nuclear magnetic resonance (NMR) relaxation. NMR relaxation times T~, off-resonance Tlp and proton-decoupled on-resonance T~p (only for carbon experiments) were measured in the temperature range from 0 to 50~ The spectral resolution in carbon cross-polarization magic angle spinning spectrum allows to treat methine, methylene and methyl carbons separately, while proton experiments provide only one integral signal from all protons at a time. The relaxation times were quantitatively analyzed by the well-established correlation function formalism and model-free approaeh. The whole set of the data could be adequately described by a model assuming three types of motion having correlation times around 10 -4, 10 -9 and 10 -~2 s. The slowest process originated from correlated eonformational transitions between different energy minima, the intermediate process could be identified as librations within one energy minimum, and the fastest one is a fast rotation of methyl protons around the symmetry axis of methyl groups. A comparison of the dynamic behavior of lysozyme and polylysine obtained from a previous study (A. Krushelnitsky, D. Faizullin, D. Reichert, Biopolymers 73, 1-15, 2004) reveals that in the dry state both biopolymers are rigid on both fast and slow time scales. Upon hydration, lysozyme and polylysine reveal a considerable enhancement of the internal mobility, however, in different ways. The side chains of polylysine are more mobile than those of lysozyme, whereas for the backbone a reversed picture is observed. This difference correlates with structural features of lysozyme and polylysine discussed in detail. Due to the presence of a fast spin diffusion, the analysis of proton relaxation data is a more difficult task. However, our data demonstrate that the correlation functions of motion obtained from carbon and proton experiments are substantially different. We explained this by the fact that these two types of NMR relaxation experiments probe the motion of different intemuclear vectors. The comparison of the proton data with our previous results on proton relaxation times T~ measured over a wide temperature range indicates that at low temperatures lysozyme undergoes structural rearrangements affecting the amplitudes and/or activation energies of motions.

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Hydration dependence of backbone and side chain polylysine dynamics: A ¹³C solid‐state NMR and IR spectroscopy study

Abstract: The molecular dynamics of solid poly-L-lysine has been studied by the following natural abundance 13 C-NMR relaxation methods: measurements of the relaxation times

Cited by 18 publications

References 36 publications

Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by1H NMR relaxation and FTIR spectroscopy

Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by1H NMR relaxation and FTIR spectroscopy

Complex ¹H,¹³C‐NMR relaxation and computer simulation study of side‐chain dynamics in solid polylysine

Response of lysozyme internal dynamics to hydration probed by13C and1H solid-state NMR relaxation

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Hydration dependence of backbone and side chain polylysine dynamics: A 13C solid‐state NMR and IR spectroscopy study

Abstract: The molecular dynamics of solid poly-L-lysine has been studied by the following natural abundance 13 C-NMR relaxation methods: measurements of the relaxation times

Cited by 18 publications

References 36 publications

Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by1H NMR relaxation and FTIR spectroscopy

Mobility and structure of human serum albumin powders in water-acetonitrile mixtures by1H NMR relaxation and FTIR spectroscopy

Complex 1H,13C‐NMR relaxation and computer simulation study of side‐chain dynamics in solid polylysine

Response of lysozyme internal dynamics to hydration probed by13C and1H solid-state NMR relaxation

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Hydration dependence of backbone and side chain polylysine dynamics: A ¹³C solid‐state NMR and IR spectroscopy study

Complex ¹H,¹³C‐NMR relaxation and computer simulation study of side‐chain dynamics in solid polylysine