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Author: Alexander P. Demchenko
Publisher: Springer Science & Business Media
ISBN: 3642708471
Category : Science
Languages : en
Pages : 323
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Book Description
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: Alexander P. Demchenko
Publisher: Springer Science & Business Media
ISBN: 3642708471
Category : Science
Languages : en
Pages : 323
Get Book
Book Description
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: Donald M. Kirschenbaum
Publisher: Springer Science & Business Media
ISBN: 1468460870
Category : Science
Languages : en
Pages : 298
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Book Description
Once you have seen the spectrum of one protein you have seen the spectra of all pro teins. Or so it would seem. While the general characteristics of the absorption curve may appear to be similar for all proteins (i. e. , in acid and neutral solution there is a minimum at 250 nm, a maximum at 278-282 nm, and no absorption above 310 nm; in alkaline solution the maximum and minimum shift to longer wavelengths), there are subtle differences which can be seen when the spectra of many proteins are compared. It is these differences which reflect changes in amino acid content and in the milieu in which the protein has been dissolved. The spectra in this book provide samples of these subtle spectral differences and permit comparisons to be made. This book was prepared to have its index read and its contents referred to. For the reader who desires to know what a protein spectrum looks like in acid and alkaline media, after X-ray or UV irradiation, or after photo-oxidation or B-bromosuccinimide treatment, spectral representations of all these experimental situations and many others are available. The indicies were prepared to provide the maximum information with the minimum effort. In addition to an alphabetical listing, all spectra are referred to by species, tissues, and the organs from which they were taken. There are also "environmental" indicies related to the treatment the proteins received prior to having their spectra taken. Technical information concerning instrumentation is lacking.
Author: Donald M. Kirschenbaum
Publisher: Springer
ISBN:
Category : Science
Languages : en
Pages : 312
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Book Description
Once you have seen the spectrum of one protein you have seen the spectra of all pro teins. Or so it would seem. While the general characteristics of the absorption curve may appear to be similar for all proteins (i. e. , in acid and neutral solution there is a minimum at 250 nm, a maximum at 278-282 nm, and no absorption above 310 nm; in alkaline solution the maximum and minimum shift to longer wavelengths), there are subtle differences which can be seen when the spectra of many proteins are compared. It is these differences which reflect changes in amino acid content and in the milieu in which the protein has been dissolved. The spectra in this book provide samples of these subtle spectral differences and permit comparisons to be made. This book was prepared to have its index read and its contents referred to. For the reader who desires to know what a protein spectrum looks like in acid and alkaline media, after X-ray or UV irradiation, or after photo-oxidation or B-bromosuccinimide treatment, spectral representations of all these experimental situations and many others are available. The indicies were prepared to provide the maximum information with the minimum effort. In addition to an alphabetical listing, all spectra are referred to by species, tissues, and the organs from which they were taken. There are also "environmental" indicies related to the treatment the proteins received prior to having their spectra taken. Technical information concerning instrumentation is lacking.
Author: Donald Kirschenbaum
Publisher: Springer Science & Business Media
ISBN: 1468488368
Category : Science
Languages : en
Pages : 534
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Book Description
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 302
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Book Description
Author: Yukihiro Ozaki
Publisher: Academic Press
ISBN: 9780128186107
Category : Science
Languages : en
Pages : 0
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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.
Author: Rosalind Wolstenholme
Publisher: John Wiley & Sons
ISBN: 1119978289
Category : Medical
Languages : en
Pages : 464
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Book Description
An in-depth text that explores the interface between analytical chemistry and trace evidence Analytical Techniques in Forensic Science is a comprehensive guide written in accessible terms that examines the interface between analytical chemistry and trace evidence in forensic science. With contributions from noted experts on the topic, the text features a detailed introduction analysis in forensic science and then subsequent chapters explore the laboratory techniques grouped by shared operating principles. For each technique, the authors incorporate specific theory, application to forensic analytics, interpretation, forensic specific developments, and illustrative case studies. Forensic techniques covered include UV-Vis and vibrational spectroscopy, mass spectrometry and gas and liquid chromatography. The applications reviewed include evidence types such as fibers, paint, drugs and explosives. The authors highlight data collection, subsequent analysis, what information has been obtained and what this means in the context of a case. The text shows how analytical chemistry and trace evidence can problem solve the nature of much of forensic analysis. This important text: Puts the focus on trace evidence and analytical science Contains case studies that illustrate theory in practice Includes contributions from experts on the topics of instrumentation, theory, and case examples Explores novel and future applications for analytical techniques Written for undergraduate and graduate students in forensic chemistry and forensic practitioners and researchers, Analytical Techniques in Forensic Science offers a text that bridges the gap between introductory textbooks and professional level literature.
Author: Alison Rodger
Publisher: Oxford University Press, USA
ISBN: 9780198558972
Category : Science
Languages : en
Pages : 170
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Book Description
This book provides an introduction to all those who wish to use the complementary spectroscopic techniques of optical activity (circular dichroism, CD) and optical anisotropy (linear dichroism, LD) for the study of the structure of molecules and interactions between molecules in solution. It emphasizes these techniques and how to use them for both low and high molecular weight molecules. The book begins by describing the principles behind CD and LD and how these techniques can be used in the laboratory without using advanced maths or quantum mechanics. The next chapters describe how both techniques may be applied to the study of biological macromolecules and give a detailed description of how they may be used on small molecules to investigate molecular and electronic structure. The final part contains theoretical derivations of all the equations required for the applications described previously. Specific molecular examples are used to illustrate concepts and to show the reader how to use the techniques in chemical and biological systems. Circular Dichroism and Linear Dichroism is an easy guide to what a prospective user of CD needs to know and explains how LD is not merely an exotic technique only to be practiced by experienced spectroscopists, but may be routinely and usefully employed as an aid to molecular structure determination.
Author: Arne Staby
Publisher: John Wiley & Sons
ISBN: 1119031176
Category : Technology & Engineering
Languages : en
Pages : 608
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Book Description
Preparative Chromatography for Separation of Proteins addresses a wide range of modeling, techniques, strategies, and case studies of industrial separation of proteins and peptides. • Covers broad aspects of preparative chromatography with a unique combination of academic and industrial perspectives • Presents Combines modeling with compliantce useing of Quality-by-Design (QbD) approaches including modeling • Features a variety of chromatographic case studies not readily accessible to the general public • Represents an essential reference resource for academic, industrial, and pharmaceutical researchers
Author: Joseph R. Lacowicz
Publisher: Springer
ISBN: 9781475781946
Category : Science
Languages : en
Pages : 310
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Book Description
The intrinsic or natural fluorescence of proteins is perhaps the most complex area of biochemical fluorescence. Fortunately the fluorescent amino acids, phenylalanine, tyrosine and tryptophan are relatively rare in proteins. Tr- tophan is the dominant intrinsic fluorophore and is present at about one mole % in protein. As a result most proteins contain several tryptophan residues and even more tyrosine residues. The emission of each residue is affected by several excited state processes including spectral relaxation, proton loss for tyrosine, rotational motions and the presence of nearby quenching groups on the protein. Additionally, the tyrosine and tryptophan residues can interact with each other by resonance energy transfer (RET) decreasing the tyrosine emission. In this sense a protein is similar to a three-particle or mul- particle problem in quantum mechanics where the interaction between particles precludes an exact description of the system. In comparison, it has been easier to interpret the fluorescence data from labeled proteins because the fluorophore density and locations could be controlled so the probes did not interact with each other. From the origins of biochemical fluorescence in the 1950s with Prof- sor G. Weber until the mid-1980s, intrinsic protein fluorescence was more qualitative than quantitative. An early report in 1976 by A. Grindvald and I. Z. Steinberg described protein intensity decays to be multi-exponential. Attempts to resolve these decays into the contributions of individual tryp- phan residues were mostly unsuccessful due to the difficulties in resolving closely spaced lifetimes.
