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Application Of Time Resolved Tryptophan Phosphoresence Spectroscopy To Protein Folding Studies
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Book Synopsis Application of Time-resolved Tryptophan Phosphoresence Spectroscopy to Protein Folding Studies by : Vinod Subramaniam
Download or read book Application of Time-resolved Tryptophan Phosphoresence Spectroscopy to Protein Folding Studies written by Vinod Subramaniam and published by . This book was released on 1996 with total page 280 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis The Use of Time-resolved Fluorescence Spectroscopy and the Synthesis of a New Photolabile Linker to Study Protein Folding by : 劉鎮宇
Download or read book The Use of Time-resolved Fluorescence Spectroscopy and the Synthesis of a New Photolabile Linker to Study Protein Folding written by 劉鎮宇 and published by . This book was released on 2000 with total page 66 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Methods in Protein Structure and Stability Analysis by : Vladimir N. Uversky
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:
Book Synopsis Applications of Optical Spectroscopy to Studies of Protein Dynamics and Folding by : Peter Michael Wolanin
Download or read book Applications of Optical Spectroscopy to Studies of Protein Dynamics and Folding written by Peter Michael Wolanin and published by . This book was released on 2000 with total page 392 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Time-Resolved Fluorescence Spectroscopy in Biochemistry and Biology by : R. Cundall
Download or read book Time-Resolved Fluorescence Spectroscopy in Biochemistry and Biology written by R. Cundall and published by Springer Science & Business Media. This book was released on 2013-11-11 with total page 767 pages. Available in PDF, EPUB and Kindle. Book excerpt: At the time that the editors conceived the idea of trying to organize the meeting on which the contents of this volume are based and which became, in March 1980, a NATO Advanced Study Institute, the techniques of time-resolved fluorescence spectroscopy, in both the nanosecond and sub-nanosecond time-domains, might reasonably have been said to be coming of age, both in their execution and in the analysis and interpretation of the results obtained. These techniques, then as now, comprised mainly a number of pulse methods using laser, flash-lamp or, most recently, synchrotron radiation. In addition, significant developments in the more classical phase approach had also rendered that method popular, utilizing either modulation of an otherwise continuous source or, again recently, the ultra-rapid pulse rate attainable with a synchrotron source. In general terms, time-resolved fluorescence studies are capable, under appropriate conditions, of supplying direct kinetic information on both photophysics and various aspects of molecular, macromolecular and supramolecular structure and dynamics. The nanosecond and sub-nanosecond time-scales directly probed render these techniques particularly appropriate in studying relaxation and fluctuation processes in macromolecules, particularly biopolymers (e. g. proteins, nucleic acids), in supramolecular assemblies such as cell membranes, and in a variety of relatively simpler model systems.
Book Synopsis Fast Dynamics in Protein Folding by : Sersita Suzette Atienza Pabit
Download or read book Fast Dynamics in Protein Folding written by Sersita Suzette Atienza Pabit and published by . This book was released on 2004 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: ABSTRACT (cont.): The miniprotein tryptophan cage folds in 4 microseconds and sets the conditions for fast folding: a two-state reaction, a weak folding activation energy barrier, a nearly optimized free energy landscape, and pre-organized structures in the unfolded state. In ferrocytochrome c, the folding time from a compact configuration is 12 microseconds in water. Analysis of the solvent viscosity-dependence of the folding time using a model based on Kramers rate theory allowed us to identify two limiting time scales in protein folding: the time scale for solvent-coupled reorganizations and the time scale controlled by the internal friction within the protein molecule.
Book Synopsis Time Resolved Optical Methods for the Study of Protein Folding and Conformation by : Anne Gershenson
Download or read book Time Resolved Optical Methods for the Study of Protein Folding and Conformation written by Anne Gershenson and published by . This book was released on 1996 with total page 306 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Time Resolved Single Molecule Fluorescence Spectroscopy on Surface Tethered and Freely Diffusing Proteins by : Diaa Atta
Download or read book Time Resolved Single Molecule Fluorescence Spectroscopy on Surface Tethered and Freely Diffusing Proteins written by Diaa Atta and published by Forschungszentrum Jülich. This book was released on 2012 with total page 143 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Protein Fluorescence by : Joseph R. Lacowicz
Download or read book Protein Fluorescence written by Joseph R. Lacowicz and published by Springer Science & Business Media. This book was released on 2006-04-18 with total page 320 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Book Synopsis Tryptophanyl-tRNA Synthetase and Its Role in the Incorporation of New Intrinsic Fluorescent Probes Into Proteins by : Christopher Warren Victor Hogue
Download or read book Tryptophanyl-tRNA Synthetase and Its Role in the Incorporation of New Intrinsic Fluorescent Probes Into Proteins written by Christopher Warren Victor Hogue and published by . This book was released on 1994 with total page 568 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Applications of Tryptophan Triplet State Spectroscopy to Studies of Protein Dynamics by : Christopher James Fischer
Download or read book Applications of Tryptophan Triplet State Spectroscopy to Studies of Protein Dynamics written by Christopher James Fischer and published by . This book was released on 2000 with total page 244 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Spectroscopy of Tryptophan in Electron Transfer and Membrane Protein Folding by : Ignacio Lopez Pena
Download or read book Spectroscopy of Tryptophan in Electron Transfer and Membrane Protein Folding written by Ignacio Lopez Pena and published by . This book was released on 2017 with total page 180 pages. Available in PDF, EPUB and Kindle. Book excerpt: The tryptophan fluorescence of proteins has been widely used to examine protein structure, ligand binding, and conformational changes. The triplet state is also well suited for examining protein structure and dynamics because of its long lifetime in some proteins, up to seconds. This dissertation focuses on several aspects of the tryptophan triplet, especially the photochemistry and photophysics of this chromophore in electron transfer and membrane protein folding. Chapter 3 describes the role of the tryptophan triplet state in mediating intermolecular electron transfer (ET). The ET rate across large distances is slow relative to a typical fluorescence lifetime. The photooxidation reaction of tryptophan in mutants of apo- and Zn(II)azurin is shown to involve the triplet state via measurements of triplet absorption and phosphorescence in the presence of an external electron acceptor. The formation of neutral radical is demonstrated to coincide with quenched phosphorescence. The formation kinetics of the triplet state and neutral radical were modeled, and the results of 1×10^7 and 8×10^5 sec-1, respectively, agree with a proposed intermolecular ET pathway (~18 Å) along 10 covalent bonds and two through-space steps. The tryptophan triplet decay kinetics are known to be different in D2O compared to H2O. This isotope effect is correlated with local solvent accessibility, and can be used to examine changes in hydration during membrane protein folding. Chapter 4 describes experiments on a model tryptophan compound, a membrane-associated peptide (melittin), and a transmembrane protein (OmpA). An isotope effect was present when tryptophan was exposed to bulk solvent, such as in unfolded melittin kH2O/kD2O=0.71, but disappeared when buried in a bilayer, such as in folded melittin kH2O/kD2O=1.07. Additionally, when OmpA was bound to the native molecular chaperone Skp, an isotope effect was absent kH2O/kD2O=1.0 . These results suggest Skp plays a role in desolvating OmpA, allowing OmpA to fold into the bilayer more easily. These data indicate that triplet photophysics may be a general tool to determine changes in hydration for proteins. Finally, spectroscopy of protein chromophores, including tryptophan, and prosthetic groups reveals local structure and dynamics. Chapter 5 discusses applications of UV and visible resonance Raman spectroscopy to proteins.
Book Synopsis Time-resolved Infrared and Fluorescence Spectroscopic Studies of Protein Dynamics and Structure by : Arnaldo L. Serrano
Download or read book Time-resolved Infrared and Fluorescence Spectroscopic Studies of Protein Dynamics and Structure written by Arnaldo L. Serrano and published by . This book was released on 2013 with total page 182 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Principles of Fluorescence Spectroscopy by : Joseph R. Lakowicz
Download or read book Principles of Fluorescence Spectroscopy written by Joseph R. Lakowicz and published by Springer Science & Business Media. This book was released on 2007-12-05 with total page 961 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Book Synopsis Protein Conformational Dynamics by : Ke-li Han
Download or read book Protein Conformational Dynamics written by Ke-li Han and published by Springer Science & Business Media. This book was released on 2014-01-20 with total page 488 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book discusses how biological molecules exert their function and regulate biological processes, with a clear focus on how conformational dynamics of proteins are critical in this respect. In the last decade, the advancements in computational biology, nuclear magnetic resonance including paramagnetic relaxation enhancement, and fluorescence-based ensemble/single-molecule techniques have shown that biological molecules (proteins, DNAs and RNAs) fluctuate under equilibrium conditions. The conformational and energetic spaces that these fluctuations explore likely contain active conformations that are critical for their function. More interestingly, these fluctuations can respond actively to external cues, which introduces layers of tight regulation on the biological processes that they dictate. A growing number of studies have suggested that conformational dynamics of proteins govern their role in regulating biological functions, examples of this regulation can be found in signal transduction, molecular recognition, apoptosis, protein / ion / other molecules translocation and gene expression. On the experimental side, the technical advances have offered deep insights into the conformational motions of a number of proteins. These studies greatly enrich our knowledge of the interplay between structure and function. On the theoretical side, novel approaches and detailed computational simulations have provided powerful tools in the study of enzyme catalysis, protein / drug design, protein / ion / other molecule translocation and protein folding/aggregation, to name but a few. This work contains detailed information, not only on the conformational motions of biological systems, but also on the potential governing forces of conformational dynamics (transient interactions, chemical and physical origins, thermodynamic properties). New developments in computational simulations will greatly enhance our understanding of how these molecules function in various biological events.
Author :Joseph R. Lacowicz Publisher :Springer Science & Business Media ISBN 13 :9780306464515 Total Pages :340 pages Book Rating :4.4/5 (645 download)
Book Synopsis Protein Fluorescence by : Joseph R. Lacowicz
Download or read book Protein Fluorescence written by Joseph R. Lacowicz and published by Springer Science & Business Media. This book was released on 2000-11-30 with total page 340 pages. Available in PDF, EPUB and Kindle. Book excerpt: This sixth volume in the highly regarded series is an essential addition to libraries serving analytical chemists, spectroscopists, biochemists, and biophysicists. Maintaining the high standards set by its predecessors, Protein Fluorescence presents twelve state-of-the-art chapters by some of the most respected researchers in the field.
Book Synopsis Time-resolved Laser Spectroscopy in Biochemistry III by : Joseph R. Lakowicz
Download or read book Time-resolved Laser Spectroscopy in Biochemistry III written by Joseph R. Lakowicz and published by . This book was released on 1992 with total page 834 pages. Available in PDF, EPUB and Kindle. Book excerpt:
