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Hydration structures of proteins = a...

Nakasako, Masayoshi.

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Hydration structures of proteins = atomic details /

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Hydration structures of proteins/ by Masayoshi Nakasako.
其他題名:	atomic details /
作者:	Nakasako, Masayoshi.
出版者:	Tokyo :Springer Japan : : 2021.,
面頁冊數:	xviii, 309 p. :ill., digital ;24 cm.
內容註:	Introduction -- Biophysical methods to visualize hydration structures of proteins -- Hydration structures inside proteins -- Hydration layer around proteins -- Structural characteristics in local hydration -- Prediction of hydration structures -- Network of hydrogen bonds around proteins -- Dipole-Dipole interactions in hydration layer -- Hydration structure changes of proteins at work -- Energy landscape and hydration of proteins.
Contained By:	Springer Nature eBook
標題:	Hydration. -
電子資源:	https://doi.org/10.1007/978-4-431-56919-0
ISBN:	9784431569190

Hydration structures of proteins = atomic details /
Nakasako, Masayoshi.

Hydration structures of proteinsatomic details /[electronic resource] :by Masayoshi Nakasako. - Tokyo :Springer Japan :2021. - xviii, 309 p. :ill., digital ;24 cm. - Soft and biological matter,2213-1744. - Soft and biological matter..

Introduction -- Biophysical methods to visualize hydration structures of proteins -- Hydration structures inside proteins -- Hydration layer around proteins -- Structural characteristics in local hydration -- Prediction of hydration structures -- Network of hydrogen bonds around proteins -- Dipole-Dipole interactions in hydration layer -- Hydration structure changes of proteins at work -- Energy landscape and hydration of proteins.

This book describes hydration structures of proteins by combining experimental results with theoretical considerations. It is designed to introduce graduate students and researchers to microscopic views of the interactions between water and biological macromolecules and to provide them with an overview of the field. Topics on protein hydration from the past 25 years are examined, most of which involve crystallography, fluorescence measurements, and molecular dynamics simulations. In X-ray crystallography and molecular dynamics simulations, recent advances have accelerated the study of hydration structures over the entire surface of proteins. Experimentally, crystal structure analysis at cryogenic temperatures is advantageous in terms of visualizing the positions of hydration water molecules on the surfaces of proteins in their frozen-hydrated crystals. A set of massive data regarding hydration sites on protein surfaces provides an appropriate basis, enabling us to identify statistically significant trends in geometrical characteristics. Trajectories obtained from molecular dynamics simulations illustrate the motion of water molecules in the vicinity of protein surfaces at sufficiently high spatial and temporal resolution to study the influences of hydration on protein motion. Together with the results and implications of these studies, the physical principles of the measurement and simulation of protein hydration are briefly summarized at an undergraduate level. Further, the author presents recent results from statistical approaches to characterizing hydrogen-bond geometry in local hydration structures of proteins. The book equips readers to better understand the structures and modes of interaction at the interface between water and proteins. Referred to as "hydration structures", they are the subject of much discussion, as they may help to answer the question of why water is indispensable for life at the molecular and atomic level.

ISBN: 9784431569190

Standard No.: 10.1007/978-4-431-56919-0doiSubjects--Topical Terms:

738666
Hydration.

LC Class. No.: QD431 / .N35 2021

Dewey Class. No.: 572.6

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505 0 $a Introduction -- Biophysical methods to visualize hydration structures of proteins -- Hydration structures inside proteins -- Hydration layer around proteins -- Structural characteristics in local hydration -- Prediction of hydration structures -- Network of hydrogen bonds around proteins -- Dipole-Dipole interactions in hydration layer -- Hydration structure changes of proteins at work -- Energy landscape and hydration of proteins.
520 $a This book describes hydration structures of proteins by combining experimental results with theoretical considerations. It is designed to introduce graduate students and researchers to microscopic views of the interactions between water and biological macromolecules and to provide them with an overview of the field. Topics on protein hydration from the past 25 years are examined, most of which involve crystallography, fluorescence measurements, and molecular dynamics simulations. In X-ray crystallography and molecular dynamics simulations, recent advances have accelerated the study of hydration structures over the entire surface of proteins. Experimentally, crystal structure analysis at cryogenic temperatures is advantageous in terms of visualizing the positions of hydration water molecules on the surfaces of proteins in their frozen-hydrated crystals. A set of massive data regarding hydration sites on protein surfaces provides an appropriate basis, enabling us to identify statistically significant trends in geometrical characteristics. Trajectories obtained from molecular dynamics simulations illustrate the motion of water molecules in the vicinity of protein surfaces at sufficiently high spatial and temporal resolution to study the influences of hydration on protein motion. Together with the results and implications of these studies, the physical principles of the measurement and simulation of protein hydration are briefly summarized at an undergraduate level. Further, the author presents recent results from statistical approaches to characterizing hydrogen-bond geometry in local hydration structures of proteins. The book equips readers to better understand the structures and modes of interaction at the interface between water and proteins. Referred to as "hydration structures", they are the subject of much discussion, as they may help to answer the question of why water is indispensable for life at the molecular and atomic level.
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