Download or read book Development of Advanced Chemometric Methods for the Analysis of Deep UV Resonance Raman Spectra of Proteins written by John Simpson and published by . This book was released on 2009 with total page 101 pages. Available in PDF, EPUB and Kindle. Book excerpt: Ultra violet resonance Raman (UVRR) is a powerful spectroscopic technique for determining the secondary structural content of proteins in solution. However, the analyses of UVRR spectra can be problematic due to the difficulty of determining the pure secondary structure Raman spectra. The use of multi-excitation datasets can help to alleviate the difficulty in determining the pure secondary structure Raman spectra, but due to increasing spectral resolution as excitation wavelength increases, multi-excitation datasets are notoriously difficult to align spectral features. In addition, the subtraction of the water band can be difficult when relying on an internal intensity standard. To address these difficulties we demonstrate the use of a series of chemometric methods. To determine the pure secondary structure Raman spectra, we demonstrate the use of multivariate curve resolution using the alternating least squares algorithm (MCRALS) with a multi-excitation data set. To alleviate mis-alignment in multi-excitation data, we demonstrate the use of correlation optimized warping (COW). We also propose a new water band subtraction method which will reliably determine the water band concentration and remove it, without an over subtraction. Finally, we demonstrate the use of parallel factor analysis (PARAFAC) for the characterization of the behavior of the flavonoid quercetin in solution with the protein bovine serum albumin.
Download or read book Development of Advanced Chemometric Methods for Analysis of Deep ultraviolet Resonance Raman and Circular Dichroism Spectroscopic Data for Protein Secondary Structure Determination written by Olayinka Oshokoya and published by . This book was released on 2015 with total page 132 pages. Available in PDF, EPUB and Kindle. Book excerpt: Determination of protein secondary structure ([alpha]-helical, [beta]-sheet, and disordered motifs) has become an area of great importance in biochemistry and biophysics as protein secondary structure is directly related to protein function and protein related diseases. While NMR and x-ray crystallography can predict placement of each atom in proteins to within an angstrom, optical methods (CD, Raman, IR) are the preferred techniques for rapid evaluation of protein secondary structure content. Such techniques require calibration data to predict unknown protein secondary structure content where accuracy may be improved with the application of multivariate analysis. We compare protein secondary structure predictions obtained from multivariate analysis of ultraviolet resonance Raman (UVRR) and circular dichroism (CD) spectroscopic data using classical and partial least squares, and multivariate curve resolution-alternating least squares is made. Based on this analysis, the suggested best approach to rapid and accurate secondary structure determination is a combination of both CD and UVRR spectroscopy.
Download or read book Deep UV Resonance Raman Spectral Properties of Alpha Helical Membrane Proteins written by Anahita Zare and published by . This book was released on 2017 with total page 109 pages. Available in PDF, EPUB and Kindle. Book excerpt: Membrane protein function and structure determination is vital for pharmaceutical development and disease prevention. Despite the various methods of protein structure elucidation in use, a need still exists for techniques that are of adequate resolution, rapid, inexpensive, and compatible with the membrane environment of these proteins. Deep UV resonance Raman (dUVRR) spectroscopy is an emerging structurally sensitive spectroscopic technique for analyzing membrane protein structure. The backbone amide modes are resonance enhanced in dUVRR spectra while the membrane's lipid features are not, resulting in strong membrane protein spectral features in near native environments. In order to better define dUVRR spectral features of membrane proteins, a series of model helical peptides, poly(LA)7, were designed. By substituting select residues of the transmembrane region of poly(LA)7, the propensity of helical structure within a membrane has also been studied. Using these model membrane peptides in increasingly dehydrated environments (aqueous, surfactant, and bilayer), hydration depended changes in the spectra are characterized.
Download or read book Deep Ultraviolet Resonance Raman Spectroscopy of Membrane Proteins written by Christopher Halsey and published by . This book was released on 2012 with total page 95 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Vibrational Spectroscopy in Protein Research written by Yukihiro Ozaki and published by Academic Press. This book was released on 2020-05-19 with total page 609 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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
Download or read book Ultraviolet Spectroscopy of Proteins written by Alexander P. Demchenko and published by Springer Science & Business Media. This book was released on 2013-11-11 with total page 323 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Methods in Protein Structure and Stability Analysis Vibrational spectroscopy written by Vladimir N. Uversky and published by Nova Publishers. This book was released on 2007 with total page 326 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Monitoring Membrane Protein Structural Changes and Interactions Via Deep UV Resonance Raman Spectroscopy written by Mia C. Brown and published by . This book was released on 2015 with total page 94 pages. Available in PDF, EPUB and Kindle. Book excerpt: Membrane proteins perform a variety of functions within our cells. They transport nutrients and waste across the lipid barrier, transmit signals from one part of the body to another, and run our immune system. However, despite their ubiquitous and vital presence in all organisms, relatively little is known about this class of proteins compared to their soluble counterparts. In this work I have set out to use deep UV resonance Raman (DUVRR) spectroscopy to characterize structural and environmental transitions of proteins and applied the results to studies involving intramembrane proteases and their substrates. DUVRR has been used extensively to observe protein secondary structure. This work contains the results of three main studies I have conducted during my graduate career. In the first I show results from the first experiment to look simultaneously at both secondary and tertiary structure as a protein transitions from a molten globule to ordered state. In the second study tracks the structural and environmental changes of a small peptide as it transitions from a soluble, disordered state through two membrane-bound, structurally ordered states. I was then able to apply the findings of these experiments to study intramembrane proteolysis, wherein I describe substrate characteristics and their interactions with proteases.
Download or read book Dissertation Abstracts International written by and published by . This book was released on 2008 with total page 1006 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Spectroscopic Methods for Determining Protein Structure in Solution written by Henry A. Havel and published by VCH Publishers. This book was released on 1996 with total page 272 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Ultraviolet Resonance Raman Spectroscopy of Proteins and Protein Components written by Robert Allen Copeland and published by . This book was released on 1986 with total page 376 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Methods in Protein Structure and Stability Analysis written by Vladimir N. Uversky and published by Nova Publishers. This book was released on 2007 with total page 382 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Raman Spectroscopy for Chemical Analysis written by Richard L. McCreery and published by John Wiley & Sons. This book was released on 2005-02-25 with total page 451 pages. Available in PDF, EPUB and Kindle. Book excerpt: Minimaler Aufwand bei der Probenvorbereitung, hoher Informationsgehalt des Spektrums und die Möglichkeit, mit festen Proben zu arbeiten, machen die Raman-Spektroskopie zunehmend attraktiv. Wie man diese Methode mit modernster Ausrüstung effizient anwendet, zeigt Ihnen das vorliegende Buch. Im Mittelpunkt stehen neue Entwicklungen wie CCDs, Diodenlaser und Fourier-Transform-Techniken. Behandelt werden auch quantitative Analysen, die in der bisher vorhandenen Literatur häufig zu kurz kamen. (08/00)
Download or read book Infrared and Raman Characteristic Group Frequencies written by George Socrates and published by John Wiley & Sons. This book was released on 2004-06-18 with total page 386 pages. Available in PDF, EPUB and Kindle. Book excerpt: Auf dieses Nachschlagewerk wird niemand verzichten wollen, der routinemäßig IR-Spektroskopie betreibt! In die 3. Auflage wurden Moleküle und Verbindungen aufgenommen, deren Daten erst seit kurzem verfügbar sind. Erstmals finden Sie auch Raman-Daten. Erweitert wurden vor allem die Kapitel zu Makromolekülen (Polymeren und Biomolekülen), zu anorganischen Verbindungen und zum NIR. Alle Diagramme wurden neu gezeichnet. (11/00)
Download or read book Visualizing Chemistry written by National Research Council and published by National Academies Press. This book was released on 2006-06-01 with total page 222 pages. Available in PDF, EPUB and Kindle. Book excerpt: Scientists and engineers have long relied on the power of imaging techniques to help see objects invisible to the naked eye, and thus, to advance scientific knowledge. These experts are constantly pushing the limits of technology in pursuit of chemical imagingâ€"the ability to visualize molecular structures and chemical composition in time and space as actual events unfoldâ€"from the smallest dimension of a biological system to the widest expanse of a distant galaxy. Chemical imaging has a variety of applications for almost every facet of our daily lives, ranging from medical diagnosis and treatment to the study and design of material properties in new products. In addition to highlighting advances in chemical imaging that could have the greatest impact on critical problems in science and technology, Visualizing Chemistry reviews the current state of chemical imaging technology, identifies promising future developments and their applications, and suggests a research and educational agenda to enable breakthrough improvements.
Download or read book Computational and Statistical Methods for Protein Quantification by Mass Spectrometry written by Ingvar Eidhammer and published by John Wiley & Sons. This book was released on 2012-12-10 with total page 290 pages. Available in PDF, EPUB and Kindle. Book excerpt: The definitive introduction to data analysis in quantitative proteomics This book provides all the necessary knowledge about mass spectrometry based proteomics methods and computational and statistical approaches to pursue the planning, design and analysis of quantitative proteomics experiments. The author’s carefully constructed approach allows readers to easily make the transition into the field of quantitative proteomics. Through detailed descriptions of wet-lab methods, computational approaches and statistical tools, this book covers the full scope of a quantitative experiment, allowing readers to acquire new knowledge as well as acting as a useful reference work for more advanced readers. Computational and Statistical Methods for Protein Quantification by Mass Spectrometry: Introduces the use of mass spectrometry in protein quantification and how the bioinformatics challenges in this field can be solved using statistical methods and various software programs. Is illustrated by a large number of figures and examples as well as numerous exercises. Provides both clear and rigorous descriptions of methods and approaches. Is thoroughly indexed and cross-referenced, combining the strengths of a text book with the utility of a reference work. Features detailed discussions of both wet-lab approaches and statistical and computational methods. With clear and thorough descriptions of the various methods and approaches, this book is accessible to biologists, informaticians, and statisticians alike and is aimed at readers across the academic spectrum, from advanced undergraduate students to post doctorates entering the field.
Download or read book Ultraviolet Resonance Raman and Fluorescence Studies of Folded and Unfolded Conformations of the Membrane Protein OmpA written by Katheryn Marie Sanchez and published by . This book was released on 2010 with total page 230 pages. Available in PDF, EPUB and Kindle. Book excerpt: This dissertation focuses on the folding dynamics of a bacterial membrane protein, Outer Membrane Protein A (OmpA), using fluorescence and Ultraviolet resonance Raman spectroscopy. Our model [Beta]-barrel membrane protein, OmpA, contains five native anchoring Tryptophan residues. The spectroscopic properties of trp residues are highly sensitive to the local environment, making it an ideal probe for membrane protein folding studies. Utilizing trp fluorescence, refolding studies were performed on single trp mutants of OmpA to determine the thermodynamic stability of these trp mutants. The important noncovalent interactions that promote stability in OmpA are pairwise aromatic interactions and hydrogen bonds with the N1H moiety of trp. Refolding studies were also performed on truncated single-trp mutants, in which the soluble domain of the protein was removed. These studies resulted in increased stability relative to the full-length protein and suggest the absence of the soluble domain may destabilize the unfolded transmembrane domain. Ultraviolet resonance Raman spectroscopy (UVRR) is a powerful vibrational technique that can selectively probe different biological chromophores depending on excitation wavelength. Excitation wavelength dependence studies were performed on OmpA using wavelengths from 206.5 nm - 236.5 nm. This study determined an optimal excitation wavelength of 228-nm to selectively enhance signal from trp residues in OmpA. Additionally, UVRR was used to monitor changes in trp environmental hydrophobicity, hydrogen bonding, and dihedral torsion angle in different conformations of OmpA. The first UVRR spectra were collected of OmpA in a highly scattering environment and show differences in folded and unfolded conformations of the protein, showing the applicability of this technique to study membrane protein folding. UVRR spectra were collected of trp mutants of OmpA at different time points in the folding/insertion process to determine the types of noncovalent interactions with trp residues, and the folding timescales these interactions occur. Our results indicate noncovalent interactions start to form within the first 20 minutes after initiation of folding into DMPC vesicles and continue to show subtle changes over the course of the folding process. Additionally, there is evidence for interactions between trp residues and lipids, inter-residue hydrogen bonding, and amino-aromatic interactions.
