The Role of Subdomains and Intermediates in the Folding and Unfolding of T4 Lysozyme PDF Download
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Author: Jason Frederick Cellitti
Publisher:
ISBN:
Category :
Languages : en
Pages : 344
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Author: Jason Frederick Cellitti
Publisher:
ISBN:
Category :
Languages : en
Pages : 344
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Author: Manuel Llinás
Publisher:
ISBN:
Category :
Languages : en
Pages : 376
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Book Description
Author: William Dean Anderson
Publisher:
ISBN:
Category : Lysozyme
Languages : en
Pages : 184
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Book Description
Author: D. Blake Gillespie
Publisher:
ISBN:
Category : Bacteriophage T4
Languages : en
Pages : 220
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Book Description
Author:
Publisher:
ISBN:
Category : Dissertations, Academic
Languages : en
Pages : 960
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Author: Claudia Tanja Mierke
Publisher: Springer Nature
ISBN: 3030585328
Category : Science
Languages : en
Pages : 919
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Book Description
This book focuses on the mechanical properties of cells, discussing the basic concepts and processes in the fields of immunology, biology, and biochemistry. It introduces and explains state-of-the-art biophysical methods and examines the role of mechanical properties in the cell/protein interaction with the connective tissue microenvironment. The book presents a unique perspective on cellular mechanics and biophysics by combining the mechanical, biological, physical, biochemical, medical, and immunological views, highlighting the importance of the mechanical properties of cells and biophysical measurement methods. The book guides readers through the complex and growing field of cellular mechanics and biophysics, connecting and discussing research findings from different fields such as biology, cell biology, immunology, physics, and medicine. Featuring suggestions for further reading throughout and addressing a wide selection of biophysical topics, this book is an indispensable guide for graduate and advanced undergraduate students in the fields of cellular mechanics and biophysics.
Author: Katelyn Blair Connell
Publisher:
ISBN:
Category :
Languages : en
Pages : 242
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Book Description
Proteins can sample a variety of partially folded conformations during the transition between the unfolded and native states. The role of such intermediates is a matter of considerable debate, but it is clear that characterization of these partially folded species is crucial for understanding protein folding and function. A single amino acid change can convert E. coli ribonuclease H from a three-state folder that populates a kinetic intermediate to one that folds in an apparent two-state fashion. We have compared the folding trajectories of the three-state and two-state RNases H, proteins with the same native state topology but altered regional stability, using a protein engineering approach. Our data indicate that that both versions of RNase H fold through a similar trajectory with similar high-energy conformations. This suggests that formation of specific partially folded conformations may be a general feature of protein folding that can promote, rather than hinder, efficient folding. To better understand the robust role this high-energy species plays in folding, we set out to trap the transient intermediate of RNase H at equilibrium by selectively destabilizing the region of the protein known to be unfolded in this species. We find that the intermediate is undetectable in a series of HSQC's, revealing the dynamic nature of this partially folded form on the timescale of NMR detection. This result is in contrast to studies in which the structures of trapped intermediates are solved by NMR, indicating that the they are well-packed and native-like. The dynamic nature of the RNase H intermediate may be important for its role as an on-pathway, productive species that promotes efficient folding. An analogous intermediate is populated on the kinetic trajectory of RNase H from T. thermophilus, an organism that grows optimally at a temperature 30 oC higher than E. coli. To understand how two proteins that share identical structures can function in such different environments, we looked for differences in their energetics by comparing equilibrium mimics of their high-energy intermediates. We find potential differences in the dynamic properties of the intermediates, which may provide insight into how proteins with the same native structure can exhibit vastly different biophysical behavior. In contrast to globular proteins such as RNase H, repeat proteins are tandem arrays of repeating structural units that have no long-range contacts. In these modular domains, the majority of native contacts could be maintained in the face of partial unfolding. Repeat proteins therefore offer a unique architecture for exploring the extent of cooperativity and roughness on the energy landscape. To understand how a modular system builds cooperativity into its energetics, and to explore the origins and limits of this cooperativity, we studied the behavior of the Notch ankyrin domain in the optical tweezers, a single molecule mechanical tool. The forced unfolding of the Notch ankyrin domain occurs in one or two steps when manipulated in the optical tweezers. Though the unfolding pathway is heterogenous compared to that observed in bulk studies, there is a limit to the degree of uncoupling of individual repeats. We compare these results to the unfolding behavior of the Notch ankyrin domain in the atomic force microscope obtained by our collaborators for this project. This offers some insight into the apparent difference in solution and AFM unfolding of ankyrin repeat proteins.
Author:
Publisher: Academic Press
ISBN: 0080957188
Category : Science
Languages : en
Pages : 3533
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Book Description
Biophysics is a rapidly-evolving interdisciplinary science that applies theories and methods of the physical sciences to questions of biology. Biophysics encompasses many disciplines, including physics, chemistry, mathematics, biology, biochemistry, medicine, pharmacology, physiology, and neuroscience, and it is essential that scientists working in these varied fields are able to understand each other's research. Comprehensive Biophysics, Nine Volume Set will help bridge that communication gap. Written by a team of researchers at the forefront of their respective fields, under the guidance of Chief Editor Edward Egelman, Comprehensive Biophysics, Nine Volume Set provides definitive introductions to a broad array of topics, uniting different areas of biophysics research - from the physical techniques for studying macromolecular structure to protein folding, muscle and molecular motors, cell biophysics, bioenergetics and more. The result is this comprehensive scientific resource - a valuable tool both for helping researchers come to grips quickly with material from related biophysics fields outside their areas of expertise, and for reinforcing their existing knowledge. Biophysical research today encompasses many areas of biology. These studies do not necessarily share a unique identifying factor. This work unites the different areas of research and allows users, regardless of their background, to navigate through the most essential concepts with ease, saving them time and vastly improving their understanding The field of biophysics counts several journals that are directly and indirectly concerned with the field. There is no reference work that encompasses the entire field and unites the different areas of research through deep foundational reviews. Comprehensive Biophysics fills this vacuum, being a definitive work on biophysics. It will help users apply context to the diverse journal literature offering, and aid them in identifying areas for further research Chief Editor Edward Egelman (E-I-C, Biophysical Journal) has assembled an impressive, world-class team of Volume Editors and Contributing Authors. Each chapter has been painstakingly reviewed and checked for consistent high quality. The result is an authoritative overview which ties the literature together and provides the user with a reliable background information and citation resource
Author:
Publisher:
ISBN:
Category : Medicine
Languages : en
Pages : 1064
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Author:
Publisher:
ISBN:
Category : Agriculture
Languages : en
Pages : 2728
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