Unnatural Amino Acids as Vibrational Spectroscopy Probes for Protein Structure and Dynamics PDF Download
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Author: Anne Creon
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
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Author: Anne Creon
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
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Author: Henrike Müller-Werkmeister
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Ultrafast protein dynamics are of great interest for understanding the molecular basis of biochemical function. One method to study structural changes with highest time-resolution starting in the femtosecond regime is 2D-IR spectroscopy. However its application to investigate protein dynamics both with high temporal and spatial resolution is currently limited to few biological systems with intrinsic chromophores. Spectral congestion, the contribution of many similar oscillators to the same signals, makes it difficult to draw conclusions about local structural dynamics in most other proteins. ...
Author: Yukihiro Ozaki
Publisher: Academic Press
ISBN: 0128186119
Category : Science
Languages : en
Pages : 609
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Book Description
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
Author: Ileana M. Pazos
Publisher:
ISBN:
Category :
Languages : en
Pages : 364
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The structure, dynamics and function of a protein are intimately controlled by a large number of intermolecular and intramolecular interactions. Thus, achieving a quantitative and molecular-level understanding of how proteins fold and function requires experimental techniques that can 'sense' and differentiate various molecular forces and, in many cases, in a site-specific manner. To that end, the focus of this thesis work is to develop non-natural amino acid-based infrared and fluorescence probes that can be used to assess the local hydration status and electrostatic environment of proteins. First, we expand the utility of a well-known site-specific spectroscopic probe, p -cyano-phenylalanine (PheCN ), by showing that (1) its fluorescence is sensitive to the presence of various anions and can thus be used to measure the heterogeneity of the protein conformation, (2) when placed at the N-terminal end of a peptide this non-natural amino acid can be used as a pH sensor for a wide variety of applications, and (3) its nitrile stretching vibration is a microscopic reporter of how a co-solvent, such as urea and trimethylamine N-oxide, modulates the protein-water interactions. Secondly, we demonstrate that the ester carbonyl stretching vibration of the non-natural amino acids, L-aspartic acid 4-methyl ester and L-glutamic acid 5-methyl ester, can be used to site-specifically quantify the electrostatic environment of proteins as its vibrational frequency correlates linearly with the local electrostatic field. Application of this infrared probe to amyloids allows us to gain new insight into their structure and dynamics.
Author: Michael D. Fayer
Publisher: CRC Press
ISBN: 1466510137
Category : Science
Languages : en
Pages : 491
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Book Description
The advent of laser-based sources of ultrafast infrared pulses has extended the study of very fast molecular dynamics to the observation of processes manifested through their effects on the vibrations of molecules. In addition, non-linear infrared spectroscopic techniques make it possible to examine intra- and intermolecular interactions and how such interactions evolve on very fast time scales, but also in some instances on very slow time scales. Ultrafast Infrared Vibrational Spectroscopy is an advanced overview of the field of ultrafast infrared vibrational spectroscopy based on the scientific research of the leading figures in the field. The book discusses experimental and theoretical topics reflecting the latest accomplishments and understanding of ultrafast infrared vibrational spectroscopy. Each chapter provides background, details of methods, and explication of a topic of current research interest. Experimental and theoretical studies cover topics as diverse as the dynamics of water and the dynamics and structure of biological molecules. Methods covered include vibrational echo chemical exchange spectroscopy, IR-Raman spectroscopy, time resolved sum frequency generation, and 2D IR spectroscopy. Edited by a recognized leader in the field and with contributions from top researchers, including experimentalists and theoreticians, this book presents the latest research methods and results. It will serve as an excellent resource for those new to the field, experts in the field, and individuals who want to gain an understanding of particular methods and research topics.
Author: Nicholas K. Preketes
Publisher:
ISBN: 9781303603662
Category :
Languages : en
Pages : 152
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Simulations of two-dimensional infrared (2DIR) spectroscopy of several proteins are presented. Applications of 2DIR spectroscopy to protein folding, protein aggregation, and photosensing are reported. We demonstrate that 2DIR spectroscopy is an excellent probe of protein structure and dynamics. Our simulations predict future experiments as well as provide detailed explanations of previous experiments. We also present simulations of the related two-dimensional ultraviolet and two-dimensional stimulated resonance Raman spectroscopies, which are shown to provide complementary information to 2DIR spectroscopy. This thesis can be viewed as a guide for the design and analysis of future two-dimensional optical measurements on proteins.
Author: Vladimir N. Uversky
Publisher: Nova Publishers
ISBN: 9781600214042
Category : Circular dichroism
Languages : en
Pages : 382
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Author: Huong Tran Kratochvil
Publisher:
ISBN:
Category :
Languages : en
Pages : 231
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Understanding the structure and dynamics of proteins is essential to understanding their roles and functions in these physiological processes. In this thesis, I describe the implementation of an ultrafast nonlinear spectroscopic technique, two-dimensional infrared (2D IR) spectroscopy to probe the structure and dynamics of ion channels and amyloid fibers. Regarding ion channels, I describe the combination of semisynthesis, 2D IR spectroscopy and molecular dynamic (MD) simulations in addressing the longstanding question of ion permeation through the selectivity filter of a potassium ion channel. I show that ions and water alternate through the filter and that these ions cannot occupy adjacent binding sites. Furthermore, 2D IR experiments revealed a flipped state that is predicted by MD simulations but not observed in x-ray crystallography. In another aspect of this work, we show that the collapsed state of the filter is structurally different in low K+ and low pH. Moreover, our work also reveals how the large conformational motions of the protein are coupled to structural changes in the selectivity filter, as evidenced by a change in the ion occupancy. In a second research direction, I developed an optical technique to quantify photoactivatable fluorophores with fluorescence microscopy. This technique allows for the quantification of a limitless number of fluorophores, and corrects for stochastic events such as fluorescence intermittency. This work can be extended to the study of amyloids, where determining the number of proteins in a prefibrillar aggregates is necessary for understanding their roles in amyloid related diseases. Finally, using 2D IR spectroscopy we describe the effect of common solvents on the anharmonicity of small molecule chromophores. The data indicates that the carbonyl anharmonicity, and, subsequently, the Stark tuning rate, is an intrinsic property of the carbonyl vibrational probes, which have important implications on the interpretation of carbonyl vibrational frequency shifts in the condensed phase.
Author:
Publisher: Elsevier
ISBN: 0080453821
Category : Science
Languages : en
Pages : 7944
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This work presents a definitive interpretation of the current status of and future trends in natural products—a dynamic field at the intersection of chemistry and biology concerned with isolation, identification, structure elucidation, and chemical characteristics of naturally occurring compounds such as pheromones, carbohydrates, nucleic acids, and enzymes. With more than 1,800 color figures, Comprehensive Natural Products II features 100% new material and complements rather than replaces the original work (©1999). Reviews the accumulated efforts of chemical and biological research to understand living organisms and their distinctive effects on health and medicine Stimulates new ideas among the established natural products research community—which includes chemists, biochemists, biologists, botanists, and pharmacologists Informs and inspires students and newcomers to the field with accessible content in a range of delivery formats Includes 100% new content, with more than 6,000 figures (1/3 of these in color) and 40,000 references to the primary literature, for a thorough examination of the field Highlights new research and innovations concerning living organisms and their distinctive role in our understanding and improvement of human health, genomics, ecology/environment, and more Adds to the rich body of work that is the first edition, which will be available for the first time in a convenient online format giving researchers complete access to authoritative Natural Products content
Author: Tiago Buckup
Publisher: Springer
ISBN: 3030024784
Category : Science
Languages : en
Pages : 325
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Book Description
The series Topics in Current Chemistry Collections presents critical reviews from the journal Topics in Current Chemistry organized in topical volumes. The scope of coverage is all areas of chemical science including the interfaces with related disciplines such as biology, medicine and materials science. The goal of each thematic volume is to give the non-specialist reader, whether in academia or industry, a comprehensive insight into an area where new research is emerging which is of interest to a larger scientific audience. Each review within the volume critically surveys one aspect of that topic and places it within the context of the volume as a whole. The most significant developments of the last 5 to 10 years are presented using selected examples to illustrate the principles discussed. The coverage is not intended to be an exhaustive summary of the field or include large quantities of data, but should rather be conceptual, concentrating on the methodological thinking that will allow the non-specialist reader to understand the information presented. Contributions also offer an outlook on potential future developments in the field.
