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Author | Title | Accn# | Year | Item Type | Claims |
| 11 |
Fabian, Heinz |
Protein Folding and Misfolding |
I07685 |
2012 |
eBook |
|
| 12 |
Rahman, Masoud |
Protein-Nanoparticle Interactions |
I07681 |
2013 |
eBook |
|
| 13 |
Williams, Mark C |
Biophysics of DNA-Protein Interactions |
I06889 |
2011 |
eBook |
|
| 14 |
Xu, Ying |
Computational Methods for Protein Structure Prediction and Modeling |
I06814 |
2007 |
eBook |
|
| 15 |
Yakubovich, Alexander V |
Theory of Phase Transitions in Polypeptides and Proteins |
I06210 |
2011 |
eBook |
|
| 16 |
Lever, Greg |
Large-Scale Quantum-Mechanical Enzymology |
I06175 |
2015 |
eBook |
|
| 17 |
Frauenfelder, Hans |
The Physics of Proteins |
I05637 |
2010 |
eBook |
|
| 18 |
Sussman, Joel L |
From Molecules to Medicines |
I05408 |
2009 |
eBook |
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11.
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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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12.
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| Title | Protein-Nanoparticle Interactions : The Bio-Nano Interface |
| Author(s) | Rahman, Masoud;Laurent, Sophie;Tawil, Nancy;Yahia, L'Hocine;Mahmoudi, Morteza |
| Publication | Berlin, Heidelberg, Springer Berlin Heidelberg, 2013. |
| Description | X, 86 p : online resource |
| Abstract Note | In recent years, the fabrication of nanomaterials and exploration of their properties have attracted the attention of various scientific disciplines such as biology, physics, chemistry, and engineering. Although nanoparticulate systems are of significant interest in various scientific and technological areas, there is little known about the safety of these nanoscale objects. It has now been established that the surfaces of nanoparticles are immediately covered by biomolecules (e.g. proteins, ions, and enzymes) upon their entrance into a biological medium. This interaction with the biological medium modulates the surface of the nanoparticles, conferring a ???biological identity??? to their surfaces (referred to as a ???corona???), which determines the subsequent cellular/tissue responses. The new interface between the nanoparticles and the biological medium/proteins, called ???bio-nano interface,??? has been very rarely studied in detail to date, though the interest in this topic is rapidly growing. In this book, the importance of the physiochemical characteristics of nanoparticles for the properties of the protein corona is discussed in detail, followed by comprehensive descriptions of the methods for assessing the protein-nanoparticle interactions. The advantages and limitations of available corona evaluation methods (e.g. spectroscopy methods, mass spectrometry, nuclear magnetic resonance, electron microscopy, X-ray crystallography, and differential centrifugal sedimentation) are examined in detail, followed by a discussion of the possibilities for enhancing the current methods and a call for new techniques. Moreover, the advantages and disadvantages of protein-nanoparticle interaction phenomena are explored and discussed, with a focus on the biological impacts |
| ISBN,Price | 9783642375552 |
| Keyword(s) | 1. BIOCHEMISTRY
2. Biochemistry, general
3. Biological and Medical Physics, Biophysics
4. BIOLOGICAL PHYSICS
5. BIOPHYSICS
6. EBOOK
7. EBOOK - SPRINGER
8. Nanoscale science
9. Nanoscale Science and Technology
10. NANOSCIENCE
11. Nanostructures
12. NANOTECHNOLOGY
13. PHARMACOLOGY
14. Pharmacology/Toxicology
15. Protein-Ligand Interactions
16. Proteins??
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I07681 |
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On Shelf |
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13.
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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 |
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On Shelf |
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14.
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| Title | Computational Methods for Protein Structure Prediction and Modeling : Volume 1: Basic Characterization |
| Author(s) | Xu, Ying;Xu, Dong;Liang, Jie |
| Publication | New York, NY, Springer New York, 2007. |
| Description | XX, 396 p. 88 illus : online resource |
| Abstract Note | Volume one of this two volume sequence focuses on the basic characterization of known protein structures as well as structure prediction from protein sequence information. The 11 chapters provide an overview of the field, covering key topics in modeling, force fields, classification, computational methods, and struture prediction. Each chapter is a self contained review designed to cover (1) definition of the problem and an historical perspective, (2) mathematical or computational formulation of the problem, (3) computational methods and algorithms, (4) performance results, (5) existing software packages, and (6) strengths, pitfalls, challenges, and future research directions |
| ISBN,Price | 9780387683720 |
| Keyword(s) | 1. BIOINFORMATICS
2. Biological and Medical Physics, Biophysics
3. BIOLOGICAL PHYSICS
4. BIOPHYSICS
5. EBOOK
6. EBOOK - SPRINGER
7. Protein Science
8. Proteins??
9. Proteomics
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I06814 |
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On Shelf |
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15.
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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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16.
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| Title | Large-Scale Quantum-Mechanical Enzymology |
| Author(s) | Lever, Greg |
| Publication | Cham, Springer International Publishing, 2015. |
| Description | XVII, 148 p. 30 illus., 12 illus. in color : online resource |
| Abstract Note | This work??establishes linear-scaling density-functional theory?? (DFT) as a powerful tool for understanding enzyme catalysis,??one that can complement quantum mechanics/molecular mechanics (QM/MM)??and molecular dynamics??simulations. The thesis reviews benchmark studies demonstrating techniques capable of simulating entire enzymes at the ab initio quantum-mechanical level of accuracy. DFT has transformed the physical sciences by allowing researchers to perform parameter-free quantum-mechanical calculations to predict a broad range of physical and chemical properties of materials. In principle, similar methods could be applied to biological problems. However, even the simplest biological systems contain many thousands of atoms and are characterized by extremely complex configuration spaces associated with a vast number of degrees of freedom. The development of linear-scaling density-functional codes makes biological molecules accessible to quantum-mechanical calculation, but has yet to resolve the complexity of the phase space. Furthermore, these calculations on systems containing up to 2,000 atoms can capture contributions to the energy that are not accounted for in QM/MM methods (for which the Nobel prize in Chemistry was awarded in 2013), and the results presented here reveal profound shortcomings in said methods |
| ISBN,Price | 9783319193519 |
| Keyword(s) | 1. BIOINFORMATICS
2. Biological and Medical Physics, Biophysics
3. BIOLOGICAL PHYSICS
4. BIOPHYSICS
5. Computational Biology/Bioinformatics
6. EBOOK
7. EBOOK - SPRINGER
8. Enzymology
9. PHYSICAL CHEMISTRY
10. Protein Science
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 |
| I06175 |
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On Shelf |
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17.
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| Title | The Physics of Proteins : An Introduction to Biological Physics and Molecular Biophysics |
| Author(s) | Frauenfelder, Hans;Chan, Shirley S;Chan, Winnie S |
| Publication | New York, NY, Springer New York, 2010. |
| Description | XVI, 448 p. 221 illus., 7 illus. in color : online resource |
| Abstract Note | Physics and the life sciences have established new connections within the past few decades, resulting in biological physics as an established subfield with strong groups working in many physics departments. These interactions between physics and biology form a two-way street with physics providing new tools and concepts for understanding life, while biological systems can yield new insights into the physics of complex systems. To address the challenges of this interdisciplinary area, The Physics of Proteins: An Introduction to Biological Physics and Molecular Biophysics is divided into three interconnected sections. In Parts I and II, early chapters introduce the terminology and describe the main biological systems that physicists will encounter. Similarities between biomolecules, glasses, and solids are stressed with an emphasis on the fundamental concepts of living systems. The central section (Parts III and IV) delves into the dynamics of complex systems. A main theme is the realization that biological systems, in particular proteins, do not exist in unique conformations but can assume a very large number of slightly different structures. This complexity is captured in the concept of a free energy landscape and leads to the conclusion that fluctuations are crucial for the functioning of biological systems. The final chapter of this section challenges the reader to apply these concepts to a problem that appears in the current literature. An extensive series of appendices (Part V) provide descriptions of the key physical tools and analytical methods that have proven powerful in the study of the physics of proteins. The appendices are designed to be consulted throughout the section on protein dynamics without breaking the deductive flow of the logic in the central section of the book |
| ISBN,Price | 9781441910448 |
| 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. Biomedicine, general
8. BIOPHYSICS
9. EBOOK
10. EBOOK - SPRINGER
11. MEDICINE
12. Protein Science
13. Proteins??
14. Proteomics
|
| Item Type | eBook |
Multi-Media Links
Please Click here for eBook
Circulation Data
| Accession# | |
Call# | Status | Issued To | Return Due On | Physical Location |
| I05637 |
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On Shelf |
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