Molecular Biophysics for the Life Sciences [electronic resource] /
Allewell, Norma.editor.
Narhi, Linda O.editor.
Rayment, Ivan.editor.
This volume of the series Biophysics for the Life Sciences focuses on the conceptual framework and major research tools of contemporary molecular biophysics.  It is designed to enable non-specialists-both students and professionals in other fields-to understand how these approaches can be used across the biosciences and in medicine, agriculture, biotechnology, pharmaceutical development and other fields.  The scope of this volume is appropriate for advanced undergraduate and graduate courses in biophysics and biophysical chemistry.   The book begins with an overview of the development of molecular biophysics and a brief survey of  structural, physical, and chemical principles.  Subsequent chapters written by experts present, with examples, the major experimental methods: optical spectroscopy, X-ray and neutron diffraction and scattering, nuclear magnetic resonance, electron paramagnetic resonance, mass spectrometry, and single molecule methods.  The relationship between the biophysical properties of biological macromolecules and their roles as molecular machines is emphasized throughout and illustrated with three examples-DNA helicases, rotary motor ATPases, and myosin.  The concluding chapter discusses future prospects in X-ray and neutron scattering, mass spectrometry, and pharmaceutical development.    Dr. Norma M. Allewell is Professor of Cell Biology and Molecular Genetics and Affiliate Professor of Chemistry and Biochemistry at the University of Maryland, where she served as Dean of the College of Chemical and Life Sciences for a decade. Her research focuses on protein structure, function and dynamics, and metabolic regulatory mechanisms and diseases.   Dr. Linda Narhi is a Scientific Executive Director in the Product Attribute Science Group at Amgen, where her responsibilities include solution stability assessment of all protein-based therapeutic candidates, and developing and implementing predictive assays for protein stability to process, storage, and delivery conditions.   Dr. Ivan Rayment is Professor of Biochemistry at the University of Wisconsin-Madison, where he holds the Michael G. Rossmann Professorship in Biochemistry. He has a wide range of interests in structural biology and has made seminal contributions to our understanding of the structural basis of motility, enzyme evolution, cobalamin biosynthesis, and transposition.
Description based upon print version of record.
Preface; About the Editors; Contents; Contributors; Chapter 1: Introduction; 1.1 What Is Biophysics?; 1.2 How Did Biophysics Develop?; 1.3 The Experimental Tools of Molecular Biophysics; 1.4 The Role of Computation in Biophysics; 1.5 Biological Macromolecules as Molecular Machines; 1.6 Examples of Molecular Machines; 1.7 Future Prospects; 1.8 Other Volumes in this Series; References; Chapter 2: Structural, Physical, and Chemical Principles; 2.1 The Molecules of the Cell; 2.2 The Importance of Three-Dimensional Structure; 2.3 Macromolecular Folding and Assembly
2.4 Thermodynamic and Kinetic Principles2.4.1 Energies, Equilibrium Constants, and Rates; 2.5 An Example: The Energetics of Protein Folding; 2.6 Applications to Protein Pharmaceutics; 2.7 Relating Structure, Energetics, and Function; References; Part I:The Experimental Tools of Molecular Biophysics; Chapter 3: Optical Spectroscopic Methods for the Analysis of Biological Macromolecules; 3.1 Introduction; 3.1.1 Physical Basis of Light Spectroscopy; 3.1.2 Theory of Light Scattering; 3.2 Chapter Overview; 3.2.1 Light Absorbance; 3.2.1.1 Introduction; 3.2.1.2 Applications; Detection
Concentration DeterminationStructural Determination; Other Chromophores; 3.2.1.3 Concluding Comments on UV Absorbance; 3.2.2 Circular Dichroism; 3.2.2.1 Theory; 3.2.2.2 Applications; Secondary Structure; Tertiary Structure; Conformational Changes in Proteins; DNA Conformation and Conformational Changes; Quantitative Comparison of CD Spectrum; Protein Binding; 3.2.2.3 Emerging CD Technology; Synchrotron Radiation Circular Dichroism; Vibrational Circular Dichroism; Concluding Comments on CD; 3.2.3 Fluorescence; 3.2.3.1 Theory; 3.2.3.2 Applications; Intrinsic Fluorescence; Protein Conformation
Fluorescence QuenchingExtrinsic Fluorescence; Red Edge Excitation of Fluorescence; Förster (Fluorescence) Resonance Energy Transfer; Fluorescence Microscopy; Solid-State Fluorescence; Use of Fluorescence Detection in High Performance Liquid Chromatography; Other Applications; 3.2.3.3 Concluding Comments on the Use of Fluorescence; 3.2.4 FTIR; 3.2.4.1 Theory; 3.2.4.2 Applications; Protein Secondary Structure Analysis; Tertiary Structure; FTIR Difference Spectroscopy; H/D Exchange for Dynamic Structure Analysis; Protein Folding and Stability; 3.2.4.3 Data Analysis
3.2.4.4 Concluding Comments on FTIR3.2.5 Raman; 3.2.5.1 Theory; Peptide Bond; Tyr; Trp; Cys; His; DNA; 3.2.5.2 Applications; Protein Conformation; Protein Dynamics; DNA Conformation; Deconvolution of Raman Spectra; Raman Microscopy; 3.2.5.3 Emerging Raman Technologies; 3.2.5.4 Concluding Comments on Raman Spectroscopy; 3.2.6 Light Scattering; 3.2.6.1 Theory; 3.2.6.2 Applications; Static Light Scattering; Dynamic Light Scattering; Other Applications of Light Scattering; Other Techniques; 3.2.6.3 Concluding Comments on Light Scattering; 3.3 Chapter Summary; References
Chapter 4: Diffraction and Scattering by X-Rays and Neutrons
Includes bibliographical references and index.
This volume of the series Biophysics for the Life Sciences focuses on the conceptual framework and major research tools of contemporary molecular biophysics.  It is designed to enable non-specialists-both students and professionals in other fields-to understand how these approaches can be used across the biosciences and in medicine, agriculture, biotechnology, pharmaceutical development and other fields.  The scope of this volume is appropriate for advanced undergraduate and graduate courses in biophysics and biophysical chemistry.   The book begins with an overview of the development of molecular biophysics and a brief survey of  structural, physical, and chemical principles.  Subsequent chapters written by experts present, with examples, the major experimental methods: optical spectroscopy, X-ray and neutron diffraction and scattering, nuclear magnetic resonance, electron paramagnetic resonance, mass spectrometry, and single molecule methods.  The relationship between the biophysical properties of biological macromolecules and their roles as molecular machines is emphasized throughout and illustrated with three examples-DNA helicases, rotary motor ATPases, and myosin.  The concluding chapter discusses future prospects in X-ray and neutron scattering, mass spectrometry, and pharmaceutical development.    Dr. Norma M. Allewell is Professor of Cell Biology and Molecular Genetics and Affiliate Professor of Chemistry and Biochemistry at the University of Maryland, where she served as Dean of the College of Chemical and Life Sciences for a decade. Her research focuses on protein structure, function and dynamics, and metabolic regulatory mechanisms and diseases.   Dr. Linda Narhi is a Scientific Executive Director in the Product Attribute Science Group at Amgen, where her responsibilities include solution stability assessment of all protein-based therapeutic candidates, and developing and implementing predictive assays for protein stability to process, storage, and delivery conditions.   Dr. Ivan Rayment is Professor of Biochemistry at the University of Wisconsin-Madison, where he holds the Michael G. Rossmann Professorship in Biochemistry. He has a wide range of interests in structural biology and has made seminal contributions to our understanding of the structural basis of motility, enzyme evolution, cobalamin biosynthesis, and transposition.
Biology-Technique.
Biophysics.
Biological physics.
Biotechnology.
Spectroscopy.
Microscopy.
Pharmaceutical technology.
Biological Techniques.
Biological and Medical Physics, Biophysics.
Biotechnology.
Spectroscopy and Microscopy.
Pharmaceutical Sciences/Technology.