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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
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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: 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: 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: 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: Joseph R. Lakowicz
Publisher: Springer Science & Business Media
ISBN: 0387463127
Category : Science
Languages : en
Pages : 961
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Book Description
The third edition of this established classic text reference builds upon the strengths of its very popular predecessors. Organized as a broadly useful textbook Principles of Fluorescence Spectroscopy, 3rd edition maintains its emphasis on basics, while updating the examples to include recent results from the scientific literature. The third edition includes new chapters on single molecule detection, fluorescence correlation spectroscopy, novel probes and radiative decay engineering. Includes a link to Springer Extras to download files reproducing all book artwork, for easy use in lecture slides. This is an essential volume for students, researchers, and industry professionals in biophysics, biochemistry, biotechnology, bioengineering, biology and medicine.
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.
Author: Gordon G. Hammes
Publisher: John Wiley & Sons
ISBN: 0471733547
Category : Science
Languages : en
Pages : 192
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Book Description
An introduction to the physical principles of spectroscopy and their applications to the biological sciences Advances in such fields as proteomics and genomics place new demands on students and professionals to be able to apply quantitative concepts to the biological phenomena that they are studying. Spectroscopy for the Biological Sciences provides students and professionals with a working knowledge of the physical chemical aspects of spectroscopy, along with their applications to important biological problems. Designed as a companion to Professor Hammes's Thermodynamics and Kinetics for the Biological Sciences, this approachable yet thorough text covers the basic principles of spectroscopy, including: * Fundamentals of spectroscopy * Electronic spectra * Circular dichroism and optical rotary dispersion * Vibration in macromolecules (IR, Raman, etc.) * Magnetic resonance * X-ray crystallography * Mass spectrometry With a minimum of mathematics and a strong focus on applications to biology, this book will prepare current and future professionals to better understand the quantitative interpretation of biological phenomena and to utilize these tools in their work.
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 302
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Book Description
