Protein Dynamics Studied by Ultrafast Visible and Infrared Laser Spectroscopy PDF Download
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Author: Yuri V. Kholodenko
Publisher:
ISBN:
Category :
Languages : en
Pages : 370
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Book Description
Author: Yuri V. Kholodenko
Publisher:
ISBN:
Category :
Languages : en
Pages : 370
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Book Description
Author: Luuk Joost Gerard Wouter van Wilderen
Publisher:
ISBN: 9789086591046
Category :
Languages : en
Pages : 147
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Book Description
Author: Ilya Joseph Finkelstein
Publisher:
ISBN:
Category :
Languages : en
Pages : 366
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Book Description
Author: Michael D. Fayer
Publisher: CRC Press
ISBN: 1466510137
Category : Science
Languages : en
Pages : 491
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Book Description
The advent of laser-based sources of ultrafast infrared pulses has extended the study of very fast molecular dynamics to the observation of processes manifested through their effects on the vibrations of molecules. In addition, non-linear infrared spectroscopic techniques make it possible to examine intra- and intermolecular interactions and how such interactions evolve on very fast time scales, but also in some instances on very slow time scales. Ultrafast Infrared Vibrational Spectroscopy is an advanced overview of the field of ultrafast infrared vibrational spectroscopy based on the scientific research of the leading figures in the field. The book discusses experimental and theoretical topics reflecting the latest accomplishments and understanding of ultrafast infrared vibrational spectroscopy. Each chapter provides background, details of methods, and explication of a topic of current research interest. Experimental and theoretical studies cover topics as diverse as the dynamics of water and the dynamics and structure of biological molecules. Methods covered include vibrational echo chemical exchange spectroscopy, IR-Raman spectroscopy, time resolved sum frequency generation, and 2D IR spectroscopy. Edited by a recognized leader in the field and with contributions from top researchers, including experimentalists and theoreticians, this book presents the latest research methods and results. It will serve as an excellent resource for those new to the field, experts in the field, and individuals who want to gain an understanding of particular methods and research topics.
Author: Niall Simpson
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
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Book Description
Proteins are complex molecular machines that facilitate the chemical reactions fundamental to life. Their functions are encoded in a linear sequence of amino acids, of which only 20 species are found in nature. Yet the functional and structural diversity accessible through these building blocks is vast. Molecular and atomic-level protein studies have been crucial to our understanding of health and treatment of disease, with increasingly sophisticated experimental and computational methods continuing to provide new information with which to advance medicine. However, the requirement for more detailed understanding of proteins has risen through the emergence of multi-antibiotic-resistant bacteria and also through the potential to design synthetic proteins of novel function. Paradigms of protein function have evolved significantly since early studies, though few all-encompassing descriptions have been proposed, owing to the complex, dynamic structures of these large biomolecules. Presently, the relationship between protein structural motions at different timescales appears to hold vital significance to the elusive aspects of biological mechanisms. No single measurement technique is capable of accessing the multitude of timescales over which protein motions occur, and thus concerted investigation is necessary. Observation of dynamics at the femtosecond-picosecond timescale has only recently become possible through the development of new experimental techniques, allowing a new class of protein motions to be investigated. In this thesis, the advanced technique of two-dimensional infrared spectroscopy (2DIR) is employed to study three biomolecular systems with implications to ubiquitous protein interactions. The aims of these investigations are, firstly, to demonstrate the suitability of 2DIR spectroscopy in gathering novel dynamic information from biological systems that is not accessible via other methods, and secondly, to derive the potential physical significance of these dynamics as they relate to biological function. A description of the underlying theory of 2DIR is presented in this Chapter, along with the considerations that must be made in the application of such a technique to complex biological case-studies. In Chapter (2), descriptions are given for the experimental setups used to acquire infrared spectra, specifically, Fourier transform infrared (FTIR), pump-probe and 2DIR spectroscopies. In Chapter (3) the catalytic-site dynamics of two closely-related haem proteins are each studied by monitoring the vibrational evolution of a nitric oxide (NO) probe molecule bound to the haem centre. A comparison of the active site dynamics is performed in order to correlate the observed differences with discrepancies between the protein reaction mechanisms. Chapter (4) explores the potential of a coenzyme with high protein-binding promiscuity to serve as an intrinsic reporter of the dynamics that occur at substrate binding sites. Infrared analysis and categorisation of the free coenzyme molecule is performed in order to establish its effectiveness as a probe. In Chapter (5), method-development strategies are proposed for the extraction of 2DIR data from large, complex protein-protein systems, with the objective of expanding the range of interactions on which 2DIR can effectively report. Both well-established and novel strategies are employed, and the potential and limitations of the technique are discussed in the context of these demanding case-studies. Chapter (6) draws together conclusions and an overview of progress made and discusses future directions.
Author: Michael D. Fayer
Publisher: World Scientific
ISBN: 9814355623
Category : Science
Languages : en
Pages : 383
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Book Description
This unique volume presents a comprehensive but accessible introduction to the field of ultrafast two-dimension infrared (2D IR) vibrational echo spectroscopy based on the pioneering work of Professor Michael D Fayer, Department of Chemistry, Stanford University, USA. It contains in one place a qualitative introduction to the field of 2D IR spectroscopy and a comprehensive set of scientific papers that underlie the qualitative discussion. The introductory material contains several detailed illustrations, and is based on the Centenary Lecture at the Indian Institute of Science given by Professor Fayer July 16, 2008 as part of the celebration of the 100th anniversary of the founding of IIS in Bangalore, India. The second part of the volume contains reprints of Fayer's relevant papers. The compilation will be very useful because it presents the historical background, motivation, methodology, and experimental results at a level that is accessible to the non-expert. The reprints of the scientific papers, from review articles to detailed theoretical papers, provide rigorous supporting material so that the reader can delve as deeply as desired into the subject.
Author:
Publisher:
ISBN:
Category : Dissertations, Academic
Languages : en
Pages : 868
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Book Description
Author: Bengt Nölting
Publisher: Springer Science & Business Media
ISBN: 354027278X
Category : Science
Languages : en
Pages : 222
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Book Description
First methods book which includes many detailed descriptions Absolutely needed and thus timely for the scientific community Comprises 15% more content and includes the mentioned special features
Author:
Publisher:
ISBN:
Category : Biomedical engineering
Languages : en
Pages : 100
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Book Description
Author: Paul Stevenson (Ph. D.)
Publisher:
ISBN:
Category :
Languages : en
Pages : 307
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Book Description
Proteins are the machinery of the cell, performing functions essential for life. Proteins do not operate in isolation, however. Their function is intimately coupled to their environment; changes in this environment modulate the behavior of the protein. One of the most striking examples of protein-environment coupling is the interaction between membrane proteins and membranes. These interactions govern some of the most fundamental processes in biology, yet the origins of protein-membrane coupling are not well understood. Infrared (IR) spectroscopy offers a route to non-invasively probing these interactions. However, despite sustained interest in the problem over many decades, only limited progress has been made using IR spectroscopy to study protein-membrane interactions. One of the main reasons for this is the density of information encoded into a small frequency range - many hundreds of oscillators may contribute to a signal which spans a
