Ordering effect of protein surfaces on water dynamics: NMR relaxation study

Bonechi Claudia; Tamasi Gabriella; Pardini Alessio; Donati Alessandro; Volpi Vanessa; Leone Gemma; Consumi Marco; Magnani Agnese; Rossi Claudio

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Ordering effect of protein surfaces on water dynamics: NMR relaxation study

机译：蛋白质表面对水动力学的排序作用：NMR松弛研究

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Proteins in solution affect the structural and dynamic properties of the bulk water at the protein-water interface, resulting in a contribution to the order of the hydration water. Theoretical and experimental NMR relaxation methods were developed to study the dynamic properties of water molecules in the protein hydration shell. Water non-selective and selective relaxation rates, were shown to be sensitive to contributions from ordered solvent molecules at protein surface. The average rotational correlation time of water molecules in the protein hydration shell was determined for three protein systems of different size: ribonuclease A, human serum albumin and fibrinogen. The knowledge of these properties is an important step toward the determination of the size of the water ordering contributions originate in proteins systems.

机译：溶液中的蛋白质影响蛋白质 - 水界面在散装水的结构和动态性质，导致水合水的顺序贡献。开发了理论和实验性NMR弛豫方法以研究蛋白质水合壳中水分子的动态性质。水无选择性和选择性松弛率显示对蛋白质表面下有序溶剂分子的贡献敏感。确定蛋白质水合壳中的水分子的平均旋转相关时间为三种不同尺寸的三种蛋白质系统：核糖核酸酶A，人血清白蛋白和纤维蛋白原。这些特性的知识是朝向源自蛋白质系统中的水处理贡献的规模的重要一步。

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来源
《Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena》 |2019年第2019期|共7页
作者
Bonechi Claudia; Tamasi Gabriella; Pardini Alessio; Donati Alessandro; Volpi Vanessa; Leone Gemma; Consumi Marco; Magnani Agnese; Rossi Claudio;
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作者单位

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

Univ Siena Dept Biotechnol Chem &

Pharm Via Aldo Moro 2 I-53100 Siena Italy;

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原文格式 PDF
正文语种 eng
中图分类生物化学;
关键词
Protein hydration; Protein size; Water ordering contribution; Water dynamic properties; NMRD profile;

机译：蛋白质水合;蛋白质尺寸;水处理贡献;水动态特性;NMRD型材;

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专利

1. Ordering effect of protein surfaces on water dynamics: NMR relaxation study [J] . Bonechi Claudia, Tamasi Gabriella, Pardini Alessio, Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena . 2019,第期

机译：蛋白质表面对水动力学的排序作用：NMR松弛研究
2. N-15 NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins [J] . Baldellon C., Strub MP., Pauls T., Biochemistry . 1998,第28期

机译：钙载小白蛋白的N-15 NMR弛豫研究表明，与其他EF手蛋白相比，动力学紧密
3. Relaxational dynamics of water molecules at protein surface [J] . S. Dellerue, M.-C. Bellissent-Funel Chemical Physics: A Journal Devoted to Experimental and Theoretical Research Involving Problems of Both a Chemical and Physical Nature . 2000,第2a3期

机译：蛋白质表面水分子的弛豫动力学
4. Water-Protein and Ligand-Protein Interactions as Determined by Selective NMR Relaxation Studies [C] . Claudio Rossi, Silvia Martini, Maso Ricci, International conference on polymer-solvent complexes and intercalates . 2003

机译：通过选择性NMR松弛研究确定的水蛋白和配体 - 蛋白质相互作用
5. Internal dynamics of the calcium -signaling protein S100B, revealed by NMR relaxation studies. [D] . Inman, Keith Griscom. 2003

机译：NMR松弛研究揭示了钙信号蛋白S100B的内部动力学。
6. Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy [O] . Alberto Ceccon, Vitali Tugarinov, Ad Bax, -1

机译：基于弛豫的溶液NMR光谱揭示的纳米颗粒表面蛋白质的整体动力学和交换动力学
7. On the Use of Side‐Chain NMR Relaxation Data to Derive Structural and Dynamical Information on Proteins: A Case Study Using Hen Lysozyme [O] . Lorna J. Smith, Wilfred F. Gunsteren, Niels Hansen 2020

机译：关于使用侧链NMR松弛数据来导出蛋白质的结构和动态信息：用母鸡溶菌酶进行案例研究
8. NMR (Nuclear Magnetic Resonance) Relaxation of Water Protons under the Influence of Proteins and other Linear Polymers [R] . Ling, G. N., Murphy, R. C. 1982

机译：在蛋白质和其他线性聚合物的影响下核质子的核磁共振（核磁共振）松弛

Ordering effect of protein surfaces on water dynamics: NMR relaxation study

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