Applications of Tryptophan Triplet State Spectroscopy to Studies of Protein Dynamics PDF Download
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Author: Christopher James Fischer
Publisher:
ISBN:
Category :
Languages : en
Pages : 244
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Author: Christopher James Fischer
Publisher:
ISBN:
Category :
Languages : en
Pages : 244
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Book Description
Author: Vinod Subramaniam
Publisher:
ISBN:
Category :
Languages : en
Pages : 280
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Book Description
Author: Joseph R. Lakowicz
Publisher: Springer Science & Business Media
ISBN: 0306439549
Category : Science
Languages : en
Pages : 398
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Book Description
Fluorescence spectroscopy and its applications to the physical and life sciences have evolved rapidly during the past decade. The increased interest in fluorescence appears to be due to advances in time resolution, methods of data analysis and improved instrumentation. With these advances, it is now practical to perform time-resolved measurements with enough resolution to compare the results with the structural and dynamic features of mac- molecules, to probe the structures of proteins, membranes, and nucleic acids, and to acquire two-dimensional microscopic images of chemical or protein distributions in cell cultures. Advances in laser and detector technology have also resulted in renewed interest in fluorescence for clinical and analytical chemistry. Because of these numerous developments and the rapid appearance of new methods, it has become difficult to remain current on the science of fluorescence and its many applications. Consequently, I have asked the experts in particular areas of fluorescence to summarize their knowledge and the current state of the art. This has resulted in the initial three volumes of Topics in Fluorescence Spectroscopy, which is intended to be an ongoing series which summarizes, in one location, the vast literature on fluorescence spectroscopy. These first three volumes are designed to serve as an advanced text. These volumes describe the more recent techniques and technologies (Volume 1), the principles governing fluorescence and the experimental observables (Volume 2), and applications in biochemistry and biophysics (Volume 3).
Author:
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ISBN:
Category : Dissertations, Academic
Languages : en
Pages : 740
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Author: Roger L. Lundblad
Publisher: CRC Press
ISBN: 1439807817
Category : Medical
Languages : en
Pages : 370
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The activity of many biopharmaceutical polymers is dependent on conformation, and the next several years will see increased interest in the conformational analysis of these polymers resulting from the development of biosimilar or "follow-on" biological products. While a wide variety of approaches to analysis exists, finding the most viable ones wou
Author: Joseph R. Lacowicz
Publisher: Springer Science & Business Media
ISBN: 0306471027
Category : Science
Languages : en
Pages : 320
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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:
Publisher:
ISBN:
Category : Medicine
Languages : en
Pages : 1860
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Author: Joseph R. Lakowicz
Publisher:
ISBN:
Category : Science
Languages : en
Pages : 834
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Author:
Publisher:
ISBN:
Category : Chemistry
Languages : en
Pages : 2540
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Book Description
Author: Gonul Kaletunc
Publisher: CRC Press
ISBN: 9780203911785
Category : Technology & Engineering
Languages : en
Pages : 560
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Book Description
Characterization of Cereals and Flours is a state-of-the-art reference that details the latest advances to characterize the effects of manufacturing processes and storage conditions on the thermal, mechanical, and structural properties of cereal flours and their products - examining the influence of moisture absorption, storage temperature, baking, and extrusion processing on flour and cereal product texture, shelf-life, and quality. The book discusses the influence of additives on pre- and postprocessed food biopolymers; the development of databases and construction of state diagrams to illustrate the state and function of cereal flours before, during, and after production; and the current techniques in image analysis, light and electron microscopy, and NMR spectroscopy used to analyze the microstructure of cereal products. It also discusses the methods used to optimize processing parameters and formulations to produce end-products with desirable sensory and textural properties; the shelf life of cereal products; and the relationships between the sensory and physical characteristics of cereal foods.
