Research Catalog

Synchrotron radiation in the biosciences

Title: Synchrotron radiation in the biosciences / edited by B. Chance [and others].
Publication: Oxford, Eng. : Clarendon Press, ©1994.

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Status	Format	Access	Call Number	Item Location
Request for On-site Use Request Scan How do I pick up this item and when will it be ready?	Text	Use in library	QH324.9.S95 S962 1994	Off-site

Details

Additional Authors

Chance, Britton.

Description

xxxi, 784 pages : illustrations; 25 cm

Subject

Bibliography (note)

Includes bibliographical references and index.

Contents

Machine derived contents note: PART I: Crystallographic studies on macromolecular structure -- 1.1. Recent developments in studies of macromolecular structure by X-ray crystallography -- 1.2. Time-resolved macromolecular crystallography -- 1.3. Protein crystallography in Japan -- 1.4. Experience in the measurement and analysis of multiwavelength anomalous dispersion data from macromolecular crystals -- 1.5. Electrostatic interactions and conformational variability in cubic insulin crystals -- 1.6. Crystal structural analysis of tobacco necrosis virus (TNV) -- 1.7. Cryocrystallography of native and derivatized ribosomal crystals -- 1.8. Structure and function of glutathione synthetase from Escherichia coli B -- 1.9. Protein structure analyses exploiting the data collection efficiency and precision provided by the macromolecule-oriented Weissenberg camera installed at Beamline 6A2 of the Photon Factory, Tsukuba -- 1.10. Structure and function of carbonic anhydrase: synchrotron X-ray diffraction studies of human carbonic anhydrase I and inhibitor complexes -- 1.11. Structure study of hydrogenase and related proteions in sulfate-reducing bacteria -- 1.12. 'Pivot hypothesis': a signalling mechanism in a bacterial chemotaxis receptor -- 1.13. Fast Weissenberg data collection as an alternative to the Laue method in kinetic crystallography -- PART 2: More information and time-dependent studies from solution X-ray scattering -- 2.1. Solution scattering -- 2.2. Time-resolved X-ray scattering study of the allosteric transition of Escherichia coli aspartate transcarbamylase -- 2.3. The effect of point mutations on the conformational changes of the allosteric enzyme aspartate transcarbamylase from Escherichia coli -- 2.4. Dynamics of microtubules from stochastic switching to periodic swinging -- 2.5. Synchrotron radiation X-ray diffraction and cryo electron microscopy studies of vinblastine-induced polymers of purified tubulin: evaluation of the effects of magnesium concentration and temperature -- 2.6. Expression of function of calmodulin: interaction between calmodulin fragment and mastoparan -- 2.7. Use of X-ray solution scattering for a protein folding study -- 2.8. High-resolution small-angle synchrotron X-ray diffraction study on multilamellar phospholipid systems -- 2.9. Temperature-jump relaxation studies on phospholipids: structural intermediates and memory effect in phase transitions -- PART 3: Biology with neutron radiation -- 3.1. Neutrons in biology -- complementarity with X-rays -- 3.2. Hydrogen bonding and solvent in proteins -- 3.3. Neutron and X-ray scattering studies of the interactions between Ca2+-binding proteins and their regulatory targets: comparisons of troponin C and calmodulin -- 3.4. Characteristic structure of phosphatidylinositol diphosphate (PIP2) complex with bovine serum albumin and water in PIP2 bilayers -- PART 4: Recent developments in biological X-ray absorption fine-structure spectroscopy -- 4.1. Sensitive and rapid biological X-ray absorption fine-structure spectroscopy -- 4.2. X-ray absorption spectroscopy using high-brilliance photon sources -- 4.3. X-ray studies of some metalloproteins -- 4.4. A structural model for the photosynthetic oxygen-evolving manganese complex -- 4.5. X-ray absorption fine structure spectroscopy and electron paramagnetic resonance studies on the molecular structure and electronic state of the Mn cluster in photosynthetic water-splitting enzyme -- 4.6. Time-resolved structure of geminate states of myoglobin CO by X-ray absorption near-edge structure spectroscopy -- 4.7. The structure-function relationship of the active sites in haemoprotein catalysis -- 4.8. Soft X-ray absorption and X-ray magnetic dichroism in biology -- PART 5: X-ray beamlines and detectors -- 5.1. Synchrotron radiation sciences in Japan -- 5.2. Diffraction and diffuse scattering beamlines for biophysical applications at the ESRF -- 5.3. Developments in gas detectors for biophysics at the Daresbury SRS -- 5.4. X-ray television detectors -- 5.5. The development of X-ray television detectors at the Photon Factory -- PART 6: Structural studies on muscle protein, muscle contraction, and filamentous virus -- 6.1. What X-rays tell us about muscle contraction -- then and now -- 6.2. DNase I binding induces a conformational change in the actin monomer -- 6.3. X-ray diffraction studies of activation and myosin head motions in frog sartorius muscle during isotonic and isometric contraction -- 6.4. X-ray diffraction evidence for a specific actomyosin complex in live isometrically contracting frog sartorius muscle -- 6.5. Modelling structural changes of the muscle thin filaments during an isometric contraction -- 6.6. Synchrotron radiation in time-resolved X-ray diffraction studies of molecular movements in muscle -- 6.7. Frequency dependence of the variation of the X-ray diffraction pattern from tetanized frog skeletal muscle during sinusoidal length changes -- 6.8. X-ray diffraction experiments on various types of vertebrate muscle -- 6.9. Application of synchrotron radiation to studies of the contractile apparatus of single intact muscle fibres -- 6.10. Structural changes of crossbridges on contraction and relaxation induced by photolysis of caged ATP: an X-ray diffraction study at the Photon Factory -- 6.11. Structural change of the myosin head detected by electron microscopy and small-angle X-ray scattering -- 6.12. Electrostatic field around the actin filament -- 6.13. X-ray diffraction studies of the thin filaments in a contracting molluscan smooth muscle -- 6.14. Muscle diffraction at the Cornell High Energy Synchrotron Source -- 6.15. Fibre diffraction studies on filamentous viruses -- PART 7: X-ray microimaging -- 7.1. Natural imaging of biological specimens with X-ray microscopes -- 7.2. Soft X-ray microscopy at the National Synchrotron Light Source -- 7.3. X-ray microscopy: present status and future prospects -- 7.4. X-ray contact microscopy of human chromosome fibres -- 7.5. Macromolecular transport in the zymogen granule measured by quantitative X-ray -- 7.6. X-ray microscopy with multilayer mirrors: the MAXIMUM photoelectron microscope -- 7.7. Application of the X-ray zooming tube to X-ray contact microscopy -- 7.8. Hard X-ray scanning microscopy and micro X-ray absorption fine-structure spectroscopy studies on iron compounds in the enameloid of fish teeth -- 7.9. The X-ray Microscopy Resource Center at the Advanced Light Source -- PART 8: Medical applications of synchrotron radiation: angiography, computerized tomography, and others -- 8.1. Synchrotron radiation coronary angiography in humans -- 8.2. Digital subtraction angiography with synchrotron radiation in Russia -- 8.3. A K-edge subtraction coronary angiography system using the dual linearly polarized synchrotron radiation beams from an ellipsoid multipole wiggler -- 8.4. Coronary angiography at the Hamburger Synchrotronstrahlungslabor (HASYLAB) -- 8.5. Medical applications of synchrotron radiation at the National Synchrotron Light Source -- PART 9: Radiation biophysics using synchrotron radiation -- 9.1. Soft X-ray radiobiology and synchrotron radiation -- 9.2. The use of synchrotron-produced ultrasoft X-rays to model radiobiological processes -- 9.3. Radiation biology of inner cell ionization/excitation -- 9.4. Radiation damage induced in free nucleotides and sulfur-containing amino acids by monoenergetic X-rays -- 9.5. DNA damage induced by monochromatic photons from synchrotron radiation -- 9.6. Ultraviolet free-electron laser facility at Brookhaven National Laboratory -- 9.7. Biological effectiveness of low-energy electrons as revealed by synchrotron-produced soft X-rays -- 9.8. Strand breaks in DNA in buffered solution induced by monochromatic X-rays around the K-shell absorption edge of phosphorus -- 9.9. Action spectra for inactivation and mutagenesis of Bacillus subtilis spores in wavelength ranges between 0.1 and 300 nm.

ISBN

019853986X
9780198539865

LCCN

93033962

OCLC

ocm28798897
28798897
SCSB-2021059

Owning Institutions

Princeton University Library