Protein and Dyes in Confinement and Protein Dynamics Studied by Fluorescence Techniques and NMR Spectroscopy PDF Download
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Author:
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Languages : en
Pages : 200
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Author:
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ISBN:
Category :
Languages : en
Pages : 200
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Author: Gregor Jung
Publisher: Springer Science & Business Media
ISBN: 3642233775
Category : Science
Languages : en
Pages : 287
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Book Description
Fluorescent proteins are intimately connected to research in the life sciences. Tagging of gene products with fluorescent proteins has revolutionized all areas of biosciences, ranging from fundamental biochemistry to clinical oncology, to environmental research. The discovery of the Green Fluorescent Protein, its first, seminal application and the ingenious development of a broad palette of fluorescence proteins of other colours, was consequently recognised with the Nobel Prize for Chemistry in 2008. Fluorescent Proteins II highlights the physicochemical and biophysical aspects of fluorescent protein technology beyond imaging. It is tailored to meet the needs of physicists, chemists and biologists who are interested in the fundamental properties of fluorescent proteins, while also focussing on specific applications. The implementations described are cutting-edge studies and exemplify how the physical and chemical properties of fluorescent proteins can stimulate novel findings in life sciences.
Author: James N. Herron
Publisher: Springer Science & Business Media
ISBN: 1489910794
Category : Medical
Languages : en
Pages : 374
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Book Description
Proteins are still gaining importance in the pharmaceutical world, where they are used to improve our arsenal of therapeutic drugs and vaccines and as diagnostic tools. Proteins are different from "traditional" low-molecular-weight drugs. As a group, they exhibit a number of biopharmaceutical and formulation problems. These problems have drawn considerable interest from both industrial and aca demic environments, forcing pharmaceutical scientists to explore a domain previ ously examined only by peptide and protein chemists. Biopharmaceutical aspects of proteins, e.g., low oral bioavailability, have been extensively investigated. Although all possible conventional routes of ad ministration have been examined for proteins, no real, generally applicable alter native to parenteral administration in order to achieve systemic effects has yet been discovered. Several of these biopharmaceutical options have been discussed in Volume 4 of this series, Biological Barriers to Protein Delivery. Proteins are composed of many amino acids, several of which are notorious for their chemical instability. Rational design of formulations that optimize the native structure and/or bioactivity of a protein is therefore of great importance when long shelf life is required, as it is for pharmaceutical products. This issue has also been examined in two prior volumes of this series: Volume 2: Stability of Protein Pharmaceuticals (Part A) and Volume 5: Stability and Characterization of Protein and Peptide Drugs.
Author: Alexandra Albanese
Publisher:
ISBN:
Category :
Languages : en
Pages : 262
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Author: Jianyong Tang
Publisher:
ISBN:
Category :
Languages : en
Pages : 211
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Author: So Yeon Kim
Publisher:
ISBN:
Category :
Languages : en
Pages : 420
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Author: Dominik Hänni
Publisher:
ISBN:
Category :
Languages : en
Pages : 189
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Author: Megan C. Thielges
Publisher: ProQuest
ISBN: 9781109124897
Category : Cytochrome c
Languages : en
Pages : 464
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Book Description
Fluctuations in protein structure on a broad range of time scales contribute to protein function. Infrared (IR) and visible spectroscopy are well suited for the study of fast processes, and accordingly, extensive effort has been aimed toward the development of these techniques for studying protein dynamics. Unfortunately, the use of IR spectroscopy for protein studies is limited by the availability of probes for characterizing specific regions of proteins. We have been developing the use of carbon deuterium (C-D) bonds as IR probes of protein electrostatics and dynamics. The isolated frequency of C-D bonds enables their observation on the conjested background of a protein IR spectra, and introduction of C-D results in a virtually native protein. This thesis aims to develop C-D bonds as probes of proteins by incorporation and characterization of C-D bonds in ligand complexes of the enzyme dihydrofolate reductase. In addition, C-D bonds were applied toward understanding the folding of evolutionarily related cytochromes c (cyt c). In effort toward extending the technique to time-resolved studies, we initiated experiments to monitor the CO rebinding to cyt c after photolysis with step scan FTIR spectroscopy. Finally, the second aim of this thesis is the application of current nonlinear spectroscopic experiments toward novel biological questions. Specifically, we report the application of 3PEPS and transient grating spectroscopies to study the impact of sequence diversity on the dynamics of set of thermodynamically diverse antibody-fluorescein complexes. We find that the dynamics of the Ab are diverse, and observe rough correlations between conformational heterogeneity and both binding entropy and the number of somatic mutations introduced during affinity maturation.
Author: Jianrong Wu
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
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Author: Ke-li Han
Publisher: Springer Science & Business Media
ISBN: 3319029703
Category : Medical
Languages : en
Pages : 488
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Book Description
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.
