Time-resolved Infrared and Fluorescence Spectroscopic Studies of Protein Dynamics and Structure PDF Download

Author: Arnaldo L. Serrano
Publisher:
ISBN:
Category :
Languages : en
Pages : 182

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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

Author: Heinz Fabian
Publisher: Springer Science & Business Media
ISBN: 3642222307
Category : Science
Languages : en
Pages : 257

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Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Author: Alexander P. Demchenko
Publisher: Springer Science & Business Media
ISBN: 3642708471
Category : Science
Languages : en
Pages : 323

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The aim of this book is to give a comprehensive description of the basic methods used in the ultraviolet spectroscopy of proteins, to discuss new trends and development of these methods, and to analyze their different applications in the study of various aspects of protein structure and dynamics. Ultraviolet spectroscopy is one of the oldest and most popular methods in the field of biochemistry and molecular biophysics. At present, it is difficult to imagine the biochemical laboratory without a recording spectrophotometer or spectrofluorimeter. There are several hundreds of publications directly devoted to protein ultraviolet spectroscopy and in a great number of studies UV spectroscopic methods are used for the structural analysis of different proteins. Meanwhile a unified description of the theoretical basis of the methods, experimental techniques, data analysis, and generalization of results obtained in solving the specific problems of protein structure are lacking. There are three reasons for which a monograph on ultraviolet spectroscopy is needed today. Firstly, there has been significant growth in facilities of experimental technique, its precision, and versatility associated with computer data analysts. This new technique is available to a wide circle of scientists engaged in the field of protein research. Most of them are not spectroscopists and, thus, there is a need for a conceivable and precise source of information on how to use this method and what kind of data it should provide.

Author: Friedrich Siebert
Publisher: John Wiley & Sons
ISBN: 3527621350
Category : Science
Languages : en
Pages : 320

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Book Description
The authors describe basic theoretical concepts of vibrational spectroscopy, address instrumental aspects and experimental procedures, and discuss experimental and theoretical methods for interpreting vibrational spectra. It is shown how vibrational spectroscopy provides information on general aspects of proteins, such as structure, dynamics, and protein folding. In addition, the authors use selected examples to demonstrate the application of Raman and IR spectroscopy to specific biological systems, such as metalloproteins, and photoreceptors. Throughout, references to extensive mathematical and physical aspects, involved biochemical features, and aspects of molecular biology are set in boxes for easier reading. Ideal for undergraduate as well as graduate students of biology, biochemistry, chemistry, and physics looking for a compact introduction to this field.

Author: Henry A. Havel
Publisher: VCH Publishers
ISBN:
Category : Science
Languages : en
Pages : 272

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Author: Yukihiro Ozaki
Publisher: Academic Press
ISBN: 0128186119
Category : Science
Languages : en
Pages : 609

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Book Description
Vibrational Spectroscopy in Protein Research offers a thorough discussion of vibrational spectroscopy in protein research, providing researchers with clear, practical guidance on methods employed, areas of application, and modes of analysis. With chapter contributions from international leaders in the field, the book addresses basic principles of vibrational spectroscopy in protein research, instrumentation and technologies available, sampling methods, quantitative analysis, origin of group frequencies, and qualitative interpretation. In addition to discussing vibrational spectroscopy for the analysis of purified proteins, chapter authors also examine its use in studying complex protein systems, including protein aggregates, fibrous proteins, membrane proteins and protein assemblies. Emphasis throughout the book is placed on applications in human tissue, cell development, and disease analysis, with chapters dedicated to studies of molecular changes that occur during disease progression, as well as identifying changes in tissues and cells in disease studies. - Provides thorough guidance in implementing cutting-edge vibrational spectroscopic methods from international leaders in the field - Emphasizes in vivo, in situ and non-invasive analysis of proteins in biomedical and life science research more broadly - Contains chapters that address vibrational spectroscopy for the study of simple purified proteins and protein aggregates, fibrous proteins, membrane proteins and protein assemblies

Author: Vladimir N. Uversky
Publisher: Nova Publishers
ISBN: 9781600217036
Category : Science
Languages : en
Pages : 326

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Book Description
Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.

Author: Vladimir N. Uversky
Publisher: Nova Publishers
ISBN: 9781600214042
Category : Circular dichroism
Languages : en
Pages : 382

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Author: Megan C. Thielges
Publisher: ProQuest
ISBN: 9781109124897
Category : Cytochrome c
Languages : en
Pages : 464

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Book Description
Fluctuations in protein structure on a broad range of time scales contribute to protein function. Infrared (IR) and visible spectroscopy are well suited for the study of fast processes, and accordingly, extensive effort has been aimed toward the development of these techniques for studying protein dynamics. Unfortunately, the use of IR spectroscopy for protein studies is limited by the availability of probes for characterizing specific regions of proteins. We have been developing the use of carbon deuterium (C-D) bonds as IR probes of protein electrostatics and dynamics. The isolated frequency of C-D bonds enables their observation on the conjested background of a protein IR spectra, and introduction of C-D results in a virtually native protein. This thesis aims to develop C-D bonds as probes of proteins by incorporation and characterization of C-D bonds in ligand complexes of the enzyme dihydrofolate reductase. In addition, C-D bonds were applied toward understanding the folding of evolutionarily related cytochromes c (cyt c). In effort toward extending the technique to time-resolved studies, we initiated experiments to monitor the CO rebinding to cyt c after photolysis with step scan FTIR spectroscopy. Finally, the second aim of this thesis is the application of current nonlinear spectroscopic experiments toward novel biological questions. Specifically, we report the application of 3PEPS and transient grating spectroscopies to study the impact of sequence diversity on the dynamics of set of thermodynamically diverse antibody-fluorescein complexes. We find that the dynamics of the Ab are diverse, and observe rough correlations between conformational heterogeneity and both binding entropy and the number of somatic mutations introduced during affinity maturation.