NMR in Structural Biology : A Collection of Papers by Kurt Wuthrich
by Wuthrich, KurtFormat: Hardcover
Pub. Date: 1995-09-01
Publisher(s): World Scientific Pub Co Inc
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Summary
The volume presents a survey of the research by Kurt Wuthrich and his associates during the period 1965 to 1994. A selection of reprints of original papers on the use of NMR spectroscopy in structural biology is supplemented with an introduction, which outlines the foundations and the historical development of the use of NMR spectroscopy for the determination of three-dimensional structures of biological macromolecules in solution. The original papers are presented in groups highlighting protein structure determination by NMR, studies of dynamic properties and hydration of biological macromolecules, and practical applications of the NMR methodology in fields such as enzymology, transcriptional regulation, immunosuppression and protein folding.
Table of Contents
| Protein structure determination in solution by NMR spectroscopy | p. 11 |
| Nuclear magnetic resonance studies of the coordination of vanadyl complexes in solution and the rate of elimination of coordinated water molecules | p. 15 |
| High resolution proton nuclear magnetic resonance spectroscopy of cytochrome c | p. 27 |
| Assignment of the heme c resonances in the 360 MHz [superscript 1]H NMR spectra of cytochrome c | p. 45 |
| Transient proton-proton Overhauser effects in horse ferrocytochrome c | p. 59 |
| Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor | p. 62 |
| Structural interpretation of vincinal proton-proton coupling constants [actual symbol not reproducible] in the basic pancreatic trypsin inhibitor measured by two-dimensional J-resolved NMR spectroscopy | p. 80 |
| Digital filtering with a sinusoidal window function: an alternative technique for resolution enhancement in FT NMR | p. 85 |
| Two-dimensional J-resolved [superscript 1]H NMR spectroscopy of biological macromolecules | p. 89 |
| Two-dimensional spin echo correlated spectroscopy (SECSY) for [superscript 1]H NMR studies of biological macromolecules | p. 96 |
| A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules | p. 103 |
| Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation | p. 109 |
| Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of [superscript 1]H-[superscript 1]H spin-spin coupling constants in proteins | p. 114 |
| Systematic application of two-dimensional [superscript 1]H nuclear-magnetic-resonance techniques for studies of proteins 1: combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labile protons in amino acid residues | p. 122 |
| Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance | p. 132 |
| Sequential resonance assignments in protein [superscript 1]H nuclear magnetic resonance spectra: computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations | p. 141 |
| Sequential resonance assignments in protein [superscript 1]H nuclear magnetic resonance spectra: basic pancreatic trypsin inhibitor | p. 167 |
| Sequential resonance assignments in protein [superscript 1]H nuclear magnetic resonance spectra: glucagon bound to perdeuterated dodecylphosphocholine micelles | p. 187 |
| [superscript 113]Cd-[superscript 1]H spin-spin couplings in homonuclear [superscript 1]H-correlated spectroscopy of metallothionein: identification of the cysteine [superscript 1]H spin systems | p. 209 |
| Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances | p. 218 |
| Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations: application to micelle-bound glucagon | p. 244 |
| Conformation of glucagon in a lipid-water interphase by [superscript 1]H nuclear magnetic resonance | p. 264 |
| Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance | p. 292 |
| An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution | p. 305 |
| Solution conformation of proteinase inhibitor IIA from bull seminal plasma by [superscript 1]H nuclear magnetic resonance and distance geometry | p. 319 |
| Secondary structure of the [alpha]-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae determined in solution by [superscript 1]H nuclear magnetic resonance | p. 345 |
| Studies by [superscript 1]H nuclear magnetic resonance and distance geometry of the solution conformation of the [alpha]-amylase inhibitor Tendamistat | p. 350 |
| Solution of the phase problem in the X-ray diffraction method for proteins with the nuclear magnetic resonance solution structure as initial model: Patterson search and refinement for the [alpha]-amylase inhibitor Tendamistat | p. 356 |
| Conformation of [Cd[subscript 7]]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy | p. 364 |
| Origin of t[subscript 1] and t[subscript 2] ridges in 2D NMR spectra and procedures for suppression | p. 389 |
| Editing of 2D [superscript 1]H NMR spectra using X half-filters: combined use with residue-selective [superscript 15]N labeling of proteins | p. 396 |
| Extended heteronuclear editing of 2D [superscript 1]H NMR spectra of isotope-labeled proteins, using the [actual symbol not reproducible] double half filter | p. 402 |
| Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with H[subscript 2]O solutions | p. 411 |
| Reduced dimensionality in triple-resonance NMR experiments | p. 417 |
| Automated stereospecific [superscript 1]H NMR assignments and their impact on the precision of protein structure determinations in solution | p. 419 |
| Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically-directed fractional [superscript 13]C labeling | p. 427 |
| Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA | p. 434 |
| Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angleconstraints | p. 448 |
| Solution conformation of E. coli lac repressor DNA binding domain by 2D NMR: sequence location and spatial arrangement of three [alpha]-helices | p. 471 |
| The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors | p. 477 |
| Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution | p. 485 |
| Homeodomain-DNA recognition | p. 493 |
| The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution | p. 506 |
| Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy | p. 518 |
| Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor | p. 529 |
| NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor | p. 534 |
| Dynamic model of globular protein conformations based on NMR studies in solution | p. 538 |
| Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution: studies with two-dimensional nuclear magnetic resonance | p. 540 |
| Amide proton exchange in proteins by EX[subscript 1] kinetics: studies of the basic pancreatic trypsin inhibitor at variable p[superscript 2]H and temperature | p. 559 |
| Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance | p. 571 |
| Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analogue | p. 576 |
| Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins | p. 584 |
| Protein dynamics studied by rotating frame [superscript 15]N spin relaxation times | p. 596 |
| Transient hydrogen bonds identified on the surface of the NMR solution structure of hirudin | p. 610 |
| Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules | p. 625 |
| Proton exchange with internal water molecules in the protein BPTI in aqueous solution | p. 630 |
| Protein hydration in aqueous solution | p. 632 |
| Polypeptide hydration in mixed solvents at low temperatures | p. 639 |
| NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution | p. 642 |
| Hydration of biological macromolecules in solution: surface structure and molecular recognition | p. 647 |
| The X-Pro peptide bond as an NMR probe for conformational studies of flexible linear peptides | p. 661 |
| Use of amide [superscript 1]H NMR titration shifts for studies of polypeptide conformation | p. 678 |
| Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons | p. 691 |
| Destabilization of the complete protein secondary structure on binding to the chaperone GroEL | p. 700 |
| NMR determination of residual structure in a urea-denatured protein, the 434-repressor | p. 705 |
| NMR assignments as a basis for structural characterization of denatured states of globular proteins | p. 710 |
| A 1. Academic and staff appointments | p. 719 |
| A 2. Ph.D. students | p. 720 |
| A 3. Undergraduate students | p. 723 |
| A 4. Postdoctoral fellows and visiting scientists | p. 724 |
| A 5. Outside collaborations | p. 726 |
| Author Index | p. 732 |
| Subject Index | p. 734 |
| Table of Contents provided by Blackwell. All Rights Reserved. |
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