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Author | Title | Accn# | Year | Item Type | Claims |
| 1 |
Fern??ndez, Ariel |
Physics at the Biomolecular Interface |
I09945 |
2016 |
eBook |
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| 2 |
Nakasako, Masayoshi |
X-Ray Diffraction Imaging of Biological Cells |
I09683 |
2018 |
eBook |
|
| 3 |
Koshlan, Tatiana |
Mathematical Modeling of Protein Complexes |
I08862 |
2018 |
eBook |
|
| 4 |
Kr??mer, Reinhard |
Membrane Transport Mechanism |
I07955 |
2014 |
eBook |
|
| 5 |
Fabian, Heinz |
Protein Folding and Misfolding |
I07685 |
2012 |
eBook |
|
| 6 |
Williams, Mark C |
Biophysics of DNA-Protein Interactions |
I06889 |
2011 |
eBook |
|
| 7 |
Yakubovich, Alexander V |
Theory of Phase Transitions in Polypeptides and Proteins |
I06210 |
2011 |
eBook |
|
| 8 |
Sussman, Joel L |
From Molecules to Medicines |
I05408 |
2009 |
eBook |
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1.
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| Title | Physics at the Biomolecular Interface : Fundamentals for Molecular Targeted Therapy |
| Author(s) | Fern??ndez, Ariel |
| Publication | Cham, Springer International Publishing, 2016. |
| Description | XV, 483 p. 295 illus., 208 illus. in color : online resource |
| Abstract Note | This book focuses primarily on the role of interfacial forces in understanding biological phenomena at the molecular scale. By providing a suitable statistical mechanical apparatus to handle the biomolecular interface, the book becomes uniquely positioned to address core problems in molecular biophysics. It highlights the importance of interfacial tension in delineating a solution to the protein folding problem, in unravelling the physico-chemical basis of enzyme catalysis and protein associations, and in rationally designing molecular targeted therapies. Thus grounded in fundamental science, the book develops a powerful technological platform for drug discovery, while it is set to inspire scientists at any level in their careers determined to address the major challenges in molecular biophysics. The acknowledgment of how exquisitely the structure and dynamics of proteins and their aqueous environment are related attests to the overdue recognition that biomolecular phenomena cannot be effectively understood without dealing with interfacial behaviour. There is an urge to grasp how biologically relevant behaviour is shaped by the structuring of biomolecular interfaces and how interfacial tension affects the molecular events that take place in the cell. This book squarely addresses these needs from a physicist perspective. The book may serve as a monograph for practitioners and, alternatively, as an advanced textbook. Fruitful reading requires a background in physical chemistry and some basics in biophysics. The selected problems at the end of the chapters and the progression in conceptual difficulty make it a suitable textbook for a graduate level course or an elective course for seniors majoring in chemistry, physics, biomedical engineering or related disciplines |
| ISBN,Price | 9783319308524 |
| Keyword(s) | 1. Biological and Medical Physics, Biophysics
2. BIOLOGICAL PHYSICS
3. BIOPHYSICS
4. COMPLEX SYSTEMS
5. DYNAMICAL SYSTEMS
6. EBOOK
7. EBOOK - SPRINGER
8. MOLECULAR BIOLOGY
9. Molecular Medicine
10. Pharmaceutical Sciences/Technology
11. Pharmaceutical technology
12. PHYSICAL CHEMISTRY
13. Protein Structure
14. Proteins??
15. STATISTICAL PHYSICS
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I09945 |
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On Shelf |
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2.
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| Title | X-Ray Diffraction Imaging of Biological Cells |
| Author(s) | Nakasako, Masayoshi |
| Publication | Tokyo, Springer Japan, 2018. |
| Description | XX, 228 p. 96 illus., 89 illus. in color : online resource |
| Abstract Note | In this book, the author describes the development of the experimental diffraction setup and structural analysis of non-crystalline particles from material science and biology. Recent advances in X-ray free electron laser (XFEL)-coherent X-ray diffraction imaging (CXDI) experiments allow for the structural analysis of non-crystalline particles to a resolution of 7 nm, and to a resolution of 20 nm for biological materials. Now XFEL-CXDI marks the dawn of a new era in structural analys of non-crystalline particles with dimensions larger than 100 nm, which was quite impossible in the 20th century. To conduct CXDI experiments in both synchrotron and XFEL facilities, the author has developed apparatuses, named KOTOBUKI-1 and TAKASAGO-6 for cryogenic diffraction experiments on frozen-hydrated non-crystalline particles at around 66 K. At the synchrotron facility, cryogenic diffraction experiments dramatically reduce radiation damage of specimen particles and allow tomography CXDI experiments. In addition, in XFEL experiments, non-crystalline particles scattered on thin support membranes and flash-cooled can be used to efficiently increase the rate of XFEL pulses. The rate, which depends on the number density of scattered particles and the size of X-ray beams, is currently 20-90%, probably the world record in XFEL-CXDI experiments. The experiment setups and results are introduced in this book. The author has also developed software suitable for efficiently processing of diffraction patterns and retrieving electron density maps of specimen particles based on the diffraction theory used in CXDI |
| ISBN,Price | 9784431566182 |
| Keyword(s) | 1. Characterization and Evaluation of Materials
2. CRYSTALLOGRAPHY
3. Crystallography and Scattering Methods
4. EBOOK
5. EBOOK - SPRINGER
6. LASERS
7. MATERIALS SCIENCE
8. Measurement Science and Instrumentation
9. Measurement??????
10. Optics, Lasers, Photonics, Optical Devices
11. PHOTONICS
12. PHYSICAL MEASUREMENTS
13. Protein Structure
14. Proteins??
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I09683 |
|
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On Shelf |
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3.
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| Title | Mathematical Modeling of Protein Complexes |
| Author(s) | Koshlan, Tatiana;Kulikov, Kirill |
| Publication | Cham, Springer International Publishing, 2018. |
| Description | XIV, 367 p. 65 illus., 48 illus. in color : online resource |
| Abstract Note | This book is devoted to the physical and mathematical modeling of the formation of complexes of protein molecules. The models developed show remarkable sensitivity to the amino acid sequences of proteins, which facilitates experimental studies and allows one to reduce the associated costs by reducing the number of measurements required according to the developed criteria. These models make it possible to reach a conclusion about the interactions between different amino acid chains and to identify more stable sites on proteins. The models also take the phosphorylation of amino acid residues into account. At the end of the book, the authors present possible directions of application of their physical and mathematical models in clinical medicine |
| ISBN,Price | 9783319983042 |
| Keyword(s) | 1. Biological and Medical Physics, Biophysics
2. BIOLOGICAL PHYSICS
3. BIOMATHEMATICS
4. Biomedical engineering
5. Biomedical Engineering and Bioengineering
6. BIOPHYSICS
7. EBOOK
8. EBOOK - SPRINGER
9. Mathematical and Computational Biology
10. Numerical and Computational Physics, Simulation
11. PHYSICS
12. Protein Structure
13. Proteins??
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I08862 |
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On Shelf |
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4.
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| Title | Membrane Transport Mechanism : 3D Structure and Beyond |
| Author(s) | Kr??mer, Reinhard;Ziegler, Christine |
| Publication | Berlin, Heidelberg, Springer Berlin Heidelberg, 2014. |
| Description | XII, 272 p. 65 illus., 56 illus. in color : online resource |
| Abstract Note | This book provides a molecular view of membrane transport by means of numerous biochemical and biophysical techniques. The rapidly growing number of atomic structures of transporters in different conformations and the constant progress in bioinformatics have recently added deeper insights. ?? The unifying mechanism of energized solute transport across membranes is assumed to consist of the conformational cycling of a carrier protein to provide access to substrate binding sites from either side of a cellular membrane. Due to the central role of active membrane transport there is considerable interest in deciphering the principles of one of the most fundamental processes in nature: the alternating access mechanism. ?? This book brings together particularly significant structure-function studies on a variety of carrier systems from different transporter families: Glutamate symporters, LeuT-like fold transporters, MFS transporters and SMR (RND) exporters, as well as ABC-type importers. ?? The selected examples impressively demonstrate how the combination of functional analysis, crystallography, investigation of dynamics and computational studies has made it possible to create a conclusive picture, or, more precisely, ???a molecular movie???. Although we are still far from a complete molecular description of the alternating access mechanism, remarkable progress has been made from static snapshots towards membrane transport dynamics |
| ISBN,Price | 9783642538391 |
| Keyword(s) | 1. BIOINFORMATICS
2. Biological and Medical Physics, Biophysics
3. BIOLOGICAL PHYSICS
4. BIOPHYSICS
5. Cell membranes??
6. Computational Biology/Bioinformatics
7. CRYSTALLOGRAPHY
8. Crystallography and Scattering Methods
9. EBOOK
10. EBOOK - SPRINGER
11. Membrane Biology
12. Protein Structure
13. Proteins??
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I07955 |
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On Shelf |
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5.
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| Title | Protein Folding and Misfolding : Shining Light by Infrared Spectroscopy |
| Author(s) | Fabian, Heinz;Naumann, Dieter |
| Publication | Berlin, Heidelberg, Springer Berlin Heidelberg, 2012. |
| Description | XVI, 244 p : online resource |
| Abstract Note | Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems |
| ISBN,Price | 9783642222306 |
| Keyword(s) | 1. Atomic structure????
2. Atomic/Molecular Structure and Spectra
3. Biological and Medical Physics, Biophysics
4. BIOLOGICAL PHYSICS
5. Biomaterials
6. BIOPHYSICS
7. EBOOK
8. EBOOK - SPRINGER
9. Molecular structure??
10. Protein Structure
11. Proteins??
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I07685 |
|
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On Shelf |
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6.
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| Title | Biophysics of DNA-Protein Interactions : From Single Molecules to Biological Systems |
| Author(s) | Williams, Mark C;Maher, III, L. James |
| Publication | New York, NY, Springer New York, 2011. |
| Description | X, 350 p : online resource |
| Abstract Note | This book presents a concise overview of current research on the biophysics of DNA-protein interactions. A wide range of new and classical methods are presented by authors investigating physical mechanisms by which proteins interact with DNA. For example, several chapters address the mechanisms by which proteins search for and recognize specific binding sites on DNA, a process critical for cellular function. Single molecule methods such as force spectroscopy as well as fluorescence imaging and tracking are described in these chapters as well as other parts of the book that address the dynamics of protein-DNA interactions. Other important topics include the mechanisms by which proteins engage DNA sequences and/or alter DNA structure. These simple but important model interactions are then placed in the broader biological context with discussion of larger protein-DNA complexes . Topics include replication forks, recombination complexes, DNA repair interactions, and ultimately, methods to understand the chromatin context of the cell nucleus. This book will be of interest to readers who wish to explore current biophysical approaches to DNA-protein interactions across multiple levels of biological complexity |
| ISBN,Price | 9780387928081 |
| Keyword(s) | 1. BIOCHEMISTRY
2. Biochemistry, general
3. Biological and Medical Physics, Biophysics
4. BIOLOGICAL PHYSICS
5. Biomedical engineering
6. Biomedical Engineering and Bioengineering
7. BIOPHYSICS
8. CELL BIOLOGY
9. EBOOK
10. EBOOK - SPRINGER
11. MOLECULAR BIOLOGY
12. Molecular Medicine
13. Protein Structure
14. Proteins??
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I06889 |
|
|
On Shelf |
|
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7.
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| Title | Theory of Phase Transitions in Polypeptides and Proteins |
| Author(s) | Yakubovich, Alexander V |
| Publication | Berlin, Heidelberg, Springer Berlin Heidelberg, 2011. |
| Description | XIII, 121 p. 39 illus., 11 illus. in color : online resource |
| Abstract Note | There are nearly 100 000 different protein sequences encoded in the human genome, each with its own specific fold. Understanding how a newly formed polypeptide sequence finds its way to the correct fold is one of the greatest challenges in the modern structural biology. The aim of this thesis is to provide novel insights into protein folding by considering the problem from the point of view of statistical mechanics. The thesis starts by investigating the fundamental degrees of freedom in polypeptides that are responsible for the conformational transitions. This knowledge is then applied in the statistical mechanics description of helix???coil transitions in polypeptides. Finally, the theoretical formalism is generalized to the case of proteins in an aqueous environment. The major novelty of this work lies in combining (a) a formalism based on fundamental physical properties of the system and (b) the resulting possibility of describing the folding???unfolding transitions quantitatively. The clear physical nature of the formalism opens the way to further applications in a large variety of systems and processes |
| ISBN,Price | 9783642225925 |
| Keyword(s) | 1. Biological and Medical Physics, Biophysics
2. BIOLOGICAL PHYSICS
3. BIOPHYSICS
4. EBOOK
5. EBOOK - SPRINGER
6. Mathematical Methods in Physics
7. Phase transitions (Statistical physics)
8. Phase Transitions and Multiphase Systems
9. PHYSICS
10. Polymer Sciences
11. Polymers????
12. Protein Structure
13. Proteins??
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I06210 |
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On Shelf |
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