Biophysics of molecular chaperones: function, mechanisms and client protein interactions
Molecular chaperones are critical to control protein quality in all living cells. Understanding chaperone function at the atomic level, and in particular its mode of interaction with client proteins, is crucial to understanding the fundamental roles chaperones play in biology. This book fills a gap...
Gespeichert in:
Weitere Verfasser: | , , |
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Format: | Buch |
Sprache: | English |
Veröffentlicht: |
London
Royal Society of Chemistry
[2024]
|
Schriftenreihe: | New developments in NMR
29 |
Schlagworte: | |
Zusammenfassung: | Molecular chaperones are critical to control protein quality in all living cells. Understanding chaperone function at the atomic level, and in particular its mode of interaction with client proteins, is crucial to understanding the fundamental roles chaperones play in biology. This book fills a gap in the literature by comprehensively summarizing and discussing new advanced experimental techniques for their analysis. Providing a comprehensive overview of advanced biophysical methods for the characterization of molecular mechanisms of molecular chaperones, the majority of the contributions are NMR methodology. This is the method of choice for atomic resolution studies of such systems. Additional notable biophysical approaches are considered to present all relevant current developments in exploring chaperone function and the transient and dynamic interactions with their client proteins.The book is targeted at both current practitioners of structural biology and biophysical chemistry and scientists who are interested in entering the field. It could be useful for graduate students as supplementary reading |
Beschreibung: | Introduction: Molecular Chaperones and Protein Quality Control;Structural Disorder in Chaperone Functions Probed by NMR;Solution NMR Approaches for Studying Molecular Chaperones;Solution NMR Studies of Chaperone–Client Systems;Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies;NMR Study of Structure and Dynamics of Chaperone–Client Complexes;Single Molecule Fluorescence Methods for Molecular Chaperones and their Client Interactions;Visualization of Chaperone Mediated Protein Folding Using X-ray Crystallography;Studying Molecular Chaperones and their Client Interactions by Nanometer Distance Restraints from Electron Paramagnetic Resonance Spectroscopy;EPR Studies of Chaperone Interactions and Dynamics;Probing Single Chaperone Substrates;Integrative Methods to Investigate Chaperones in Regulating Protein Phase Separation and Aggregation;Structural Biology in Cells by In-cell NMR |
Beschreibung: | xviii, 394 Seiten Illustrationen, Diagramme 777 gr |
ISBN: | 9781839162824 |
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id | DE-604.BV049567997 |
illustrated | Illustrated |
index_date | 2024-07-03T23:29:50Z |
indexdate | 2024-07-20T04:35:36Z |
institution | BVB |
isbn | 9781839162824 |
language | English |
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physical | xviii, 394 Seiten Illustrationen, Diagramme 777 gr |
publishDate | 2024 |
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publisher | Royal Society of Chemistry |
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series | New developments in NMR |
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spelling | Biophysics of molecular chaperones function, mechanisms and client protein interactions edited by Sebastian Hiller (Biozentrum, University of Basel, Switzerland), Maili Liu (Chinese Academy of Sciences, Wuhan, China) and Lichun He (Chinese Academy of Sciences, Wuhan, China) London Royal Society of Chemistry [2024] xviii, 394 Seiten Illustrationen, Diagramme 777 gr txt rdacontent n rdamedia nc rdacarrier New developments in NMR 29 Introduction: Molecular Chaperones and Protein Quality Control;Structural Disorder in Chaperone Functions Probed by NMR;Solution NMR Approaches for Studying Molecular Chaperones;Solution NMR Studies of Chaperone–Client Systems;Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies;NMR Study of Structure and Dynamics of Chaperone–Client Complexes;Single Molecule Fluorescence Methods for Molecular Chaperones and their Client Interactions;Visualization of Chaperone Mediated Protein Folding Using X-ray Crystallography;Studying Molecular Chaperones and their Client Interactions by Nanometer Distance Restraints from Electron Paramagnetic Resonance Spectroscopy;EPR Studies of Chaperone Interactions and Dynamics;Probing Single Chaperone Substrates;Integrative Methods to Investigate Chaperones in Regulating Protein Phase Separation and Aggregation;Structural Biology in Cells by In-cell NMR Molecular chaperones are critical to control protein quality in all living cells. Understanding chaperone function at the atomic level, and in particular its mode of interaction with client proteins, is crucial to understanding the fundamental roles chaperones play in biology. This book fills a gap in the literature by comprehensively summarizing and discussing new advanced experimental techniques for their analysis. Providing a comprehensive overview of advanced biophysical methods for the characterization of molecular mechanisms of molecular chaperones, the majority of the contributions are NMR methodology. This is the method of choice for atomic resolution studies of such systems. Additional notable biophysical approaches are considered to present all relevant current developments in exploring chaperone function and the transient and dynamic interactions with their client proteins.The book is targeted at both current practitioners of structural biology and biophysical chemistry and scientists who are interested in entering the field. It could be useful for graduate students as supplementary reading bicssc / Magnetic resonance bicssc / Proteins bicssc / Molecular biology bisacsh / SCIENCE / Chemistry / Analytic bisacsh / SCIENCE / Life Sciences / Molecular Biology Polypeptidketten bindende Proteine (DE-588)4311255-9 gnd rswk-swf Biophysik (DE-588)4006891-2 gnd rswk-swf Polypeptidketten bindende Proteine (DE-588)4311255-9 s Biophysik (DE-588)4006891-2 s DE-604 Hiller Odermatt, Sebastian 1976- (DE-588)108979651X edt Liu, Maili edt He, Lichun (DE-588)1068840889 edt Erscheint auch als Online-Ausgabe, PDF 978-1-83916-598-6 Erscheint auch als Online-Ausgabe, EPUB 978-1-83916-599-3 New developments in NMR 29 (DE-604)BV042012135 29 |
spellingShingle | Biophysics of molecular chaperones function, mechanisms and client protein interactions New developments in NMR bicssc / Magnetic resonance bicssc / Proteins bicssc / Molecular biology bisacsh / SCIENCE / Chemistry / Analytic bisacsh / SCIENCE / Life Sciences / Molecular Biology Polypeptidketten bindende Proteine (DE-588)4311255-9 gnd Biophysik (DE-588)4006891-2 gnd |
subject_GND | (DE-588)4311255-9 (DE-588)4006891-2 |
title | Biophysics of molecular chaperones function, mechanisms and client protein interactions |
title_auth | Biophysics of molecular chaperones function, mechanisms and client protein interactions |
title_exact_search | Biophysics of molecular chaperones function, mechanisms and client protein interactions |
title_exact_search_txtP | Biophysics of molecular chaperones function, mechanisms and client protein interactions |
title_full | Biophysics of molecular chaperones function, mechanisms and client protein interactions edited by Sebastian Hiller (Biozentrum, University of Basel, Switzerland), Maili Liu (Chinese Academy of Sciences, Wuhan, China) and Lichun He (Chinese Academy of Sciences, Wuhan, China) |
title_fullStr | Biophysics of molecular chaperones function, mechanisms and client protein interactions edited by Sebastian Hiller (Biozentrum, University of Basel, Switzerland), Maili Liu (Chinese Academy of Sciences, Wuhan, China) and Lichun He (Chinese Academy of Sciences, Wuhan, China) |
title_full_unstemmed | Biophysics of molecular chaperones function, mechanisms and client protein interactions edited by Sebastian Hiller (Biozentrum, University of Basel, Switzerland), Maili Liu (Chinese Academy of Sciences, Wuhan, China) and Lichun He (Chinese Academy of Sciences, Wuhan, China) |
title_short | Biophysics of molecular chaperones |
title_sort | biophysics of molecular chaperones function mechanisms and client protein interactions |
title_sub | function, mechanisms and client protein interactions |
topic | bicssc / Magnetic resonance bicssc / Proteins bicssc / Molecular biology bisacsh / SCIENCE / Chemistry / Analytic bisacsh / SCIENCE / Life Sciences / Molecular Biology Polypeptidketten bindende Proteine (DE-588)4311255-9 gnd Biophysik (DE-588)4006891-2 gnd |
topic_facet | bicssc / Magnetic resonance bicssc / Proteins bicssc / Molecular biology bisacsh / SCIENCE / Chemistry / Analytic bisacsh / SCIENCE / Life Sciences / Molecular Biology Polypeptidketten bindende Proteine Biophysik |
volume_link | (DE-604)BV042012135 |
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