C. Woodward

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The hydrogen exchange core and protein folding

R. Li, C. Woodward, Renhao Li, 1999, Protein science : a publication of the Protein Society.

Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design

H. Edelsbrunner, Jie Liang, C. Woodward, 1998, Protein science : a publication of the Protein Society.

Is the slow exchange core the protein folding core?

C. Woodward, 1993, Trends in biochemical sciences.

Native-like interactions favored in the unfolded bovine pancreatic trypsin inhibitor have different roles in folding.

C. Woodward, Renhao Li, J. Battiste, 2002, Biochemistry.

The concentration dependence of the diffusion coefficient for bovine pancreatic trypsin inhibitor: A dynamic light scattering study of a small protein

C. Woodward, W. Gallagher, 1989, Biopolymers.

A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association.

C. Woodward, V. Roongta, K. Mayo, 1997, Biochemistry.

Hydrogen exchange of primary amide protons in basic pancreatic trypsin inhibitor: evidence for NH2 group rotation in buried asparagine side chains.

C. Woodward, E. Tüchsen, 1987, Biochemistry.

Thermodynamics of bpti folding

Clare Woodward, C. Woodward, P. Privalov, 1993, Protein science : a publication of the Protein Society.

Hydrogen exchange kinetics and internal motions in proteins and nucleic acids.

C. Woodward, B. D. Hilton, C K Woodward, 1979, Annual review of biophysics and bioengineering.

Renal receptors for calcitonin. Binding and degradation of hormone.

C. Woodward, H. Keutmann, S. Marx, 1973, The Journal of biological chemistry.

Chemical synthesis and nuclear magnetic resonance characterization of partially folded proteins.

C. Woodward, G. Bárány, E. Barbar, 1997, Methods in enzymology.

Multivalent IDP assemblies: Unique properties of LC8‐associated, IDP duplex scaffolds

Sarah A. Clark, C. Woodward, E. Barbar, 2015, FEBS letters.

Hydrogen exchange kinetics of core peptide protons in Streptomyces subtilisin inhibitor.

C. Woodward, H. Hatano, T. Inoue, 1985, Biochemistry.

Crevice‐forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: Crystal structures of F22A, Y23A, N43G, and F45A

C. Woodward, A. Wlodawer, Key‐Sun Kim, 1993, Protein Science.

Studies of hydrogen exchange in proteins. 3. The effects of the chymotrypsinogen-alpha chymotrypsin conversion on hydrogen exchange kinetics.

C. Woodward, A. Rosenberg, 1970, The Journal of biological chemistry.

Towards New Designed Proteins: Oxime Ligation of Core Modules

C. Woodward, G. Bárány, N. Carulla, 2001 .

Isolation and characterization of rcsB mutations that affect colanic acid capsule synthesis in Escherichia coli K-12

C. Woodward, V. Stout, G. Gupte, 1997, Journal of bacteriology.

Preparation of protected peptidyl thioester intermediates for native chemical ligation by Nalpha-9-fluorenylmethoxycarbonyl (Fmoc) chemistry: considerations of side-chain and backbone anchoring strategies, and compatible protection for N-terminal cysteine.

C. Woodward, D. Lelièvre, G. Bárány, 2005, The journal of peptide research : official journal of the American Peptide Society.

Solvent accessibility in folded proteins. Studies of hydrogen exchange in trypsin.

C. Woodward, A. Rosenberg, L. M. Ellis, 1975, The Journal of biological chemistry.

Acidic ribosomal proteins of Neurospora crassa.

C. Woodward, C. H. Kim, L. Taaffe, 1984, Biochimica et biophysica acta.

Pressure response of protein backbone structure. Pressure‐induced amide 15N chemical shifts in BPTI

C. Woodward, Renhao Li, K. Akasaka, 1999, Protein science : a publication of the Protein Society.

Rapid internal dynamics of BPTI is insensitive to pressure

C. Woodward, H. Yamada, S. Sareth, 2000, FEBS letters.

Hydrogen exchange kinetics of surface peptide amides in bovine pancreatic trypsin inhibitor.

C. Woodward, E. Tüchsen, Clare Woodward, 1987, Journal of molecular biology.

Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor beta-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor.

C. Woodward, P. Brandt, 1987, Biochemistry.

Structure of form III crystals of bovine pancreatic trypsin inhibitor.

C. Woodward, A. Wlodawer, G. Gilliland, 1987, Journal of molecular biology.

Hydrogen exchange and the dynamic structure of proteins

C. Woodward, I. Simon, E. Tüchsen, 1982, Molecular and Cellular Biochemistry.

Solid-phase synthesis of bovine pancreatic trypsin inhibitor (BPTI) and two analogues. A chemical approach for evaluating the role of disulfide bridges in protein folding and stability.

C. Woodward, M. Ferrer, G. Bárány, 2009, International journal of peptide and protein research.

Synthetic Approaches to Disulfide-free Circular Bovine Pancreatic Trypsin Inhibitor (c-BPTI) Analogues

C. Woodward, Judit Tulla-Puche, F. Albericio, 2006, International Journal of Peptide Research and Therapeutics.

Use of phospha-alkynes in metal aggregate synthesis. Crystal and molecular structure of the remarkable hexa-rhodium complex [Rh2Cl2{Rh(η5-C5H5)(P2C2But2)}4]

J. F. Nixon, C. Woodward, P. Hitchcock, 1987 .

Conformation, stability, and active‐site cysteine titrations of Escherichia coli D26A thioredoxin probed by Raman spectroscopy

C. Woodward, R. Tuma, G. Thomas, 1998, Protein science : a publication of the Protein Society.

Optimized methods for chemical synthesis of bovine pancreatic trypsin inhibitor (BPTI) analogues

C. Woodward, M. Ferrer, H. Pan, 1996 .

Determination of the pKa values of active-center cysteines, cysteines-32 and -35, in Escherichia coli thioredoxin by Raman spectroscopy.

C. Woodward, G. Thomas, J. Fuchs, 1993, Biochemistry.

Titratable effects of p-chloromercuriphenyl sulfonate, a thiol-attacking reagent, on glucocorticoid receptor binding.

C. Woodward, R. Harrison, E. Thompson, 1983, Biochimica et biophysica acta.

Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon.

C. Woodward, L. Ellis, P. Saurugger, 1992, Biochemistry.

Hydrogen-tritium exchange kinetics of soybean trypsin inhibitor (Kunitz). Solvent accessibility in the folded conformation.

C. Woodward, V. Bloomfield, L. M. Ellis, 1975, Biochemistry.

The conserved, buried aspartic acid in oxidized Escherichia coli thioredoxin has a pKa of 7.5. Its titration produces a related shift in global stability.

C Woodward, C. Woodward, J. Fuchs, 1991, Biochemistry.

Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink.

C. Woodward, G. Bárány, E. Barbar, 1996, Folding & design.

Solid-phase synthesis of bovine pancreatic trypsin inhibitor and analogues designed to determine the role of disulfide bridges in protein folding and stability

C. Woodward, M. Ferrer, G. Bárány, 1993 .

Assignment of the imidazole ring nitrogen protons of histidine 48 in the proton NMR spectrum of ribonuclease A in water solution.

C. Woodward, D. Patel, F. Bovey, 1975, Biochimica et biophysica acta.

Assignment of the histidine 12‐threonine 45 hydrogen‐bonded proton in the nmr spectrum of ribonuclease A in H2O

C. Woodward, D. Patel, F. Bovey, 1975, Biopolymers.

Escherichia coli glutaredoxin: cloning and overexpression, thermodynamic stability of the oxidized and reduced forms, and report of an N-terminal extended species.

C. Woodward, B. Kren, J. Fuchs, 1991, Biochemistry.

Correlation of exchangeable (NH) and nonexchangeable (C2H) histidine resonances in the proton nmr spectrum of ribonuclease A in aqueous solution

C. Woodward, D. Patel, Lita L. Canuel, 1975, Biopolymers.

The solvent dependence of hydrogen exchange kinetics of folded proteins.

C. Woodward, A. Rosenberg, L. M. Ellis, 1975, The Journal of biological chemistry.

Effect of trypsin binding on the hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor .beta.-sheet NH's

C. Woodward, I. Simon, E. Tüchsen, 1984 .

Crystal structure of a Y35G mutant of bovine pancreatic trypsin inhibitor.

A Wlodawer, C Woodward, C. Woodward, 1991, Journal of molecular biology.

E. coli Thioredoxin Stability Is Greatly Enhanced by Substitution of Aspartic Acid 26 by Alanine

C. Woodward, Y. Sung, J. Fuchs, 1990 .

Aspartic acid 26 in reduced Escherichia coli thioredoxin has a pKa > 9.

C. Woodward, J. Fuchs, E. Barbar, 1995, Biochemistry.

Crevice‐forming mutants of bovine pancreatic trypsin inhibitor: Stability changes and new hydrophobic surface

C. Woodward, A. Wlodawer, Key‐Sun Kim, 1993, Protein science : a publication of the Protein Society.

Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin.

C. Woodward, D. Ohlendorf, Judit Tulla-Puche, 2008, Journal of molecular biology.

On the molecular weight of thiosulfate sulfurtransferase.

C. Woodward, L. M. Ellis, 1975, Biochimica et biophysica acta.

Studies of hydrogen exchange in proteins. V. The correlation of ribonuclease exchange kinetics with the temperature-induced transition.

C. Woodward, A. Rosenberg, 1971, The Journal of biological chemistry.

Mechanism of surface peptide proton exchange in bovine pancreatic trypsin inhibitor. Salt effects and O-protonation.

C. Woodward, E. Tüchsen, 1985, Journal of molecular biology.

Dynamic solvent accessibility in the soybean trypsin inhibitor--trypsin complex.

C. Woodward, 1977, Journal of molecular biology.

Solvent exchange of buried water and hydrogen exchange of peptide NH groups hydrogen bonded to buried waters in bovine pancreatic trypsin inhibitor.

C. Woodward, J. Hayes, V. Copié, 1987, Biochemistry.

Advances in protein hydrogen exchange by mass spectrometry

C. Woodward, 1999 .

Hydrogen kinetics of peptide amide protons at the bovine pancreatic trypsin inhibitor protein-solvent interface.

C. Woodward, E. Tüchsen, Clare Woodward, 1985, Journal of molecular biology.

Hydrogen exchange rates in pancreatic trypsin inhibitor are not correlated to thermal stability in urea.

C. Woodward, B. D. Hilton, K. Trudeau, 1981, Biochemistry.

On the mechanism of isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor.

C. Woodward, B. D. Hilton, 1979, Biochemistry.

Nuclear magnetic resonance measurement of hydrogen exchange kinetics of single protons in basic pancreatic trypsin inhibitor.

C. Woodward, B. D. Hilton, 1978, Biochemistry.

Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor.

C. Woodward, B. D. Hilton, 1980, Biophysical journal.

Hydrogen exchange kinetics changes upon formation of the soybean trypsin inhibitor-trypsin complex.

C. Woodward, L. M. Ellis, 1975, Biochemistry.

Oxidized RNase as a protein model having no contribution to the hydrogen exchange rate from conformational restrictions.

C. Woodward, A. Rosenberg, 1970, Proceedings of the National Academy of Sciences of the United States of America.

Assignment of asparagine-44 side-chain primary amide 1H NMR resonances and the peptide amide N1H resonance of glycine-37 in basic pancreatic trypsin inhibitor.

C. Woodward, E. Tüchsen, 1987, Biochemistry.

Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor.

C. Woodward, H. Pan, E. Barbar, 1995, Biochemistry.

The slow-exchange core and protein folding.

C. Woodward, R. Li, 1998, Trends in biochemical sciences.

Dynamic structure of a highly ordered beta-sheet molten globule: multiple conformations with a stable core.

C. Woodward, E. Barbar, G. Barany, 1995, Biochemistry.

Hydrogen exchange rates and protein folding

Clare Woodward, C. Woodward, 1994 .

Local fluctuations and global unfolding of partially folded BPTI detected by NMR.

C. Woodward, V. J. Licata, E. Barbar, 1997, Biophysical chemistry.

Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor

C. Woodward, M. Ferrer, G. Barany, 1995, Nature Structural Biology.

Experimental approaches to protein folding based on the concept of a slow hydrogen exchange core.

C. Woodward, J. Battiste, E. Barbar, 2001, Journal of molecular graphics & modelling.

Native state hydrogen-exchange analysis of protein folding and protein motional domains.

C. Woodward, N. Carulla, G. Barany, 2004, Methods in enzymology.

BetaCore, a designed water soluble four‐stranded antiparallel β‐sheet protein

C. Woodward, N. Carulla, G. Barany, 2002 .

Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor

C. Woodward, H. Pan, G. Barany, 1997, Protein science : a publication of the Protein Society.

Surveying the protein folding landscape: equilibrium models for partially folded intermediates of bovine pancreatic trypsin inhibitor (BPTI)

C. Woodward, C. M. Gross, G. Barany, 2002 .

Hydrogen exchange identifies native-state motional domains important in protein folding.

C. Woodward, K. Kim, J. Fuchs, 1993, Biochemistry.

Escherichia coli thioredoxin folds into two compact forms of different stability to urea denaturation.

C. Woodward, J. Fuchs, K. Langsetmo, 1989, Biochemistry.

Linkage of thioredoxin stability to titration of ionizable groups with perturbed pKa.

K. Sharp, C. Woodward, J. Fuchs, 1991, Biochemistry.

Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution.

C. Woodward, W. Gallagher, Feng Tao, 1992, Biochemistry.

Toward new designed proteins derived from bovine pancreatic trypsin inhibitor (BPTI): covalent cross-linking of two 'core modules' by oxime-forming ligation.

C. Woodward, N. Carulla, G. Barany, 2001, Bioconjugate chemistry.

Studies of hydrogen exchange in proteins. VI. Urea effects on ribonuclease exchange kinetics leading to a general model for hydrogen exchange from folded proteins.

C. Woodward, A. Rosenberg, 1971, The Journal of biological chemistry.

A highly destabilizing mutation, G37A, of the bovine pancreatic trypsin inhibitor retains the average native conformation but greatly increases local flexibility.

Clare Woodward, Renhao Li, C. Woodward, 2002, Biochemistry.

Hydrogen exchange, core modules, and new designed proteins.

C. Woodward, N. Carulla, G. Barany, 2002, Biophysical chemistry.

Studies on membrane transport. VII. Transport of histidine through two distinct systems in the tapeworm Hymenolepis diminuta.

C. Woodward, C. P. Read, 1969, Comparative biochemistry and physiology.