Resolving Protein Dynamics by Single-molecule Fluorescence and Neutron Scattering PDF Download
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Author: Benedikt Sohmen
Publisher:
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Languages : en
Pages : 0
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Author: Benedikt Sohmen
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
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Author: Diaa Atta
Publisher: Forschungszentrum Jülich
ISBN: 3893367632
Category :
Languages : en
Pages : 143
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Author:
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ISBN:
Category :
Languages : en
Pages :
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Protein dynamics and its relation to protein function is the subject of various studies using both, theoretical and experimental techniques. In this thesis, several aspects of protein dynamics on short timescales are addressed. Motions in the pico- to nanosecond timescale have been experimentally shown to be intimately related to enzyme activity. Incoherent neutron scattering and molecular dynamics simulation are well suited and widely used to study motions on the above timescales. A prominent phenomenon in the context of this observed flexibility-activity relationship is the dynamical transition, i.e. a non-linear increase in atomic fluctuations at a characteristic transition temperature of T_0 ca. 200K. By explicitly incorporating finite resolution of neutron spectrometers in the theoretical analysis of neutron scattering experiments, a novel interpretation of the dynamical transition arises. This alternative 'frequency window' interpretation is shown to reproduce the timescale and temperature dependence of mean-square displacements calculated from MD simulations of a protein in solution. The frequency window interpretation, furthermore, offers an explanation of the experimentally observed shift of T_0 with instrumental resolution. Implications of the new interpretation for the relation between the dynamical transition and enzyme activity are discussed. Molecular dynamics simulations are further used to test the Gaussian approximation implicit in experimental data analysis. Deviations from Gaussian scattering in the calculated spectra for Q^26 Ang^{-2} are shown to be dominated by the distribution of
Author: Christoph Bräuchle
Publisher: John Wiley & Sons
ISBN: 9783527628377
Category : Science
Languages : en
Pages : 359
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Closing a gap in the literature, this handbook gathers all the information on single particle tracking and single molecule energy transfer. It covers all aspects of this hot and modern topic, from detecting virus entry to membrane diffusion, and from protein folding using spFRET to coupled dye systems, as well recent achievements in the field. Throughout, the first-class editors and top international authors present content of the highest quality, making this a must-have for physical chemists, spectroscopists, molecular physicists and biochemists.
Author: 楊承翰
Publisher:
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Category :
Languages : en
Pages :
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Author: So Yeon Kim
Publisher:
ISBN:
Category :
Languages : en
Pages : 420
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Author: Ke-li Han
Publisher: Springer Science & Business Media
ISBN: 3319029703
Category : Medical
Languages : en
Pages : 488
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Book Description
This book discusses how biological molecules exert their function and regulate biological processes, with a clear focus on how conformational dynamics of proteins are critical in this respect. In the last decade, the advancements in computational biology, nuclear magnetic resonance including paramagnetic relaxation enhancement, and fluorescence-based ensemble/single-molecule techniques have shown that biological molecules (proteins, DNAs and RNAs) fluctuate under equilibrium conditions. The conformational and energetic spaces that these fluctuations explore likely contain active conformations that are critical for their function. More interestingly, these fluctuations can respond actively to external cues, which introduces layers of tight regulation on the biological processes that they dictate. A growing number of studies have suggested that conformational dynamics of proteins govern their role in regulating biological functions, examples of this regulation can be found in signal transduction, molecular recognition, apoptosis, protein / ion / other molecules translocation and gene expression. On the experimental side, the technical advances have offered deep insights into the conformational motions of a number of proteins. These studies greatly enrich our knowledge of the interplay between structure and function. On the theoretical side, novel approaches and detailed computational simulations have provided powerful tools in the study of enzyme catalysis, protein / drug design, protein / ion / other molecule translocation and protein folding/aggregation, to name but a few. This work contains detailed information, not only on the conformational motions of biological systems, but also on the potential governing forces of conformational dynamics (transient interactions, chemical and physical origins, thermodynamic properties). New developments in computational simulations will greatly enhance our understanding of how these molecules function in various biological events.
Author: Michael E. Wall
Publisher: CRC Press
ISBN: 1439827230
Category : Science
Languages : en
Pages : 392
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Book Description
Quantitative methods are revolutionizing modern molecular and cellular biology. Groundbreaking technical advances are fueling the rapid expansion in our ability to observe, as seen in multidisciplinary studies that integrate theory, computation, experimental assays, and the control of microenvironments. Integrating new experimental and theoretical
Author: Sharona Cohen
Publisher: Springer
ISBN: 3319095587
Category : Science
Languages : en
Pages : 70
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Book Description
In this thesis single-molecule fluorescence resonance energy transfer (FRET) spectroscopy was used to study the folding of a protein that belongs to the large and important family of repeat proteins. Cohen shows that the dynamics of the expanded conformations is likely to be very fast, suggesting a spring-like motion of the whole chain. The findings shed new light on the elasticity of structure in repeat proteins, which is related to their function in binding multiple and disparate partners. This concise research summary provides useful insights for students beginning a PhD in this or a related area, and researchers entering this field.
Author: Sebastian Hiller
Publisher: Royal Society of Chemistry
ISBN: 1839165995
Category : Science
Languages : en
Pages : 344
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Book Description
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.
