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Author : Diaa Atta
Publisher : Forschungszentrum Jülich
Page : 143 pages
File Size : 40,8 Mb
Release : 2012
Category : Electronic
ISBN : 9783893367634
Author : Matteo Gabba
Publisher : Forschungszentrum Jülich
Page : 197 pages
File Size : 53,7 Mb
Release : 2014-03-28
Category : Electronic
ISBN : 9783893369430
Author : Manfred Niesert
Publisher : Forschungszentrum Jülich
Page : 161 pages
File Size : 48,6 Mb
Release : 2012
Category : Electronic
ISBN : 9783893367863
Author : Zhendong Fu
Publisher : Forschungszentrum Jülich
Page : 239 pages
File Size : 50,6 Mb
Release : 2012
Category : Electronic
ISBN : 9783893367979
Author : Naveen Kumar Chogondahalli Muniraju
Publisher : Forschungszentrum Jülich
Page : 209 pages
File Size : 43,9 Mb
Release : 2012
Category : Electronic
ISBN : 9783893368020
Author : Boris Lorenz
Publisher : Forschungszentrum Jülich
Page : 139 pages
File Size : 52,6 Mb
Release : 2012
Category : Electronic
ISBN : 9783893367795
Author : Christoph July
Publisher : Forschungszentrum Jülich
Page : 131 pages
File Size : 46,9 Mb
Release : 2012
Category : Electronic
ISBN : 9783893367917
Author : Thomas Brückel
Publisher : Forschungszentrum Jülich
Page : 197 pages
File Size : 52,8 Mb
Release : 2012
Category : Electronic
ISBN : 9783893368075
Author : Paul Ferdinand Baumeister
Publisher : Forschungszentrum Jülich
Page : 233 pages
File Size : 40,5 Mb
Release : 2012
Category : Electronic
ISBN : 9783893368365
Author : Artur Glavic
Publisher : Forschungszentrum Jülich
Page : 173 pages
File Size : 52,7 Mb
Release : 2012
Category : Electronic
ISBN : 9783893368037
Author : Anonim
Publisher : Forschungszentrum Jülich
Page : 183 pages
File Size : 44,8 Mb
Release : 2012
Category : Electronic
ISBN : 9783893367900
Author : Chris Gell,David Brockwell,Alastair Smith
Publisher : Oxford University Press on Demand
Page : 279 pages
File Size : 46,7 Mb
Release : 2006-08-17
Category : Science
ISBN : 9780198529422
This is a practical introduction to single molecule fluorescence experiments, the analysis of the data, and applications of the techniques to the study of biological structure and function.
Author : Anonim
Publisher : Academic Press
Page : 720 pages
File Size : 53,6 Mb
Release : 2010-07-09
Category : Science
ISBN : 0123814839
Single molecule tools have begun to revolutionize the molecular sciences, from biophysics to chemistry to cell biology. They hold the promise to be able to directly observe previously unseen molecular heterogeneities, quantitatively dissect complex reaction kinetics, ultimately miniaturize enzyme assays, image components of spatially distributed samples, probe the mechanical properties of single molecules in their native environment, and "just look at the thing" as anticipated by the visionary Richard Feynman already half a century ago. Single Molecule Tools, Part B: Super-Resolution, Particle Tracking, Multiparameter, and Force Based Methods captures a snapshot of this vibrant, rapidly expanding field, presenting articles from pioneers in the field intended to guide both the newcomer and the expert through the intricacies of getting single molecule tools. Includes time-tested core methods and new innovations applicable to any researcher employing single molecule tools Methods included are useful to both established researchers and newcomers to the field Relevant background and reference information given for procedures can be used as a guide to developing protocols in a number of disciplines
Author : Sharona Cohen
Publisher : Springer
Page : 59 pages
File Size : 46,8 Mb
Release : 2015-10-17
Category : Science
ISBN : 9783319095585
In this thesis single-molecule fluorescence resonance energy transfer (FRET) spectroscopy was used to study the folding of a protein that belongs to the large and important family of repeat proteins. Cohen shows that the dynamics of the expanded conformations is likely to be very fast, suggesting a spring-like motion of the whole chain. The findings shed new light on the elasticity of structure in repeat proteins, which is related to their function in binding multiple and disparate partners. This concise research summary provides useful insights for students beginning a PhD in this or a related area, and researchers entering this field.
Author : Joseph R. Lacowicz
Publisher : Springer Science & Business Media
Page : 310 pages
File Size : 47,6 Mb
Release : 2006-04-18
Category : Science
ISBN : 9780306471025
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.