Professor Jon Waltho
Gibson Chair in Biophysics
Tel: 0114 222 2717
Our laboratory focuses on the use of high field NMR spectroscopy to determine the structure and function of proteins and how they fold from their fully unfolded states. Our studies address both fundamental aspects of protein biophysics and dynamics, and the investigation of the biomedical targets and their inhibition.
Recent highlights include the structure determination and characterisation of the solution dynamics of the human intracellular cysteine proteinase inhibitor stefin A. Proteins of this family inhibit enzymes central to the invasion of the body by foreign organisms (e.g. trypanosomes that cause African Sleeping sickness) and the entry of metastatic cancer cells into new tissues. In addition, the absence of the protein stefin B was recently the first identified genetic cause of epilepsy. Structure and dynamic measurements of stefins provide insights into means of developing small molecule pharmaceuticals that mimic the protective function of this class of proteins.
Understanding how proteins fold is both a major goal from a viewpoint of fundamental biochemistry, and is of growing biomedical importance owing its implication in a variety of neurodegenerative diseases. Diseases ranging from Alzheimer’s, through amyloid angiopathy to the prion diseases, CJD and BSE, appear to utilise partially and misfolded states of proteins. We have shown how NMR can be used to determine structural and dynamic information of such states, which provide a basis for identifying where and how to interrupt amyloidogenesis before the onset of neurodegeneration. We focus on three proteins in this regard, cystatin C, human prion protein and phosphoglycerate kinase (PGK).
Enzymes that catalyse phosphoryl transfer include kinases, ATPases and phosphatases, and therefore constitute arguably the most important group of enzymes. They increase the reaction rate by up to 1020-fold - a truly remarkable rate increase. Studies by our group, reported in Angewandte Chemie 2017 56:4110, use a combination of X-ray crystallography, NMR, and computational analysis, using metal fluorides as analogues of the phosphate group. They show how these enzymes use a combination of precise geometrical positioning, charge balance, and control of hydrogen bonds, to achieve their rate enhancements. They also show how much we still have to learn.
Structural biology, NMR, enzymology, kinetics, protein folding, prions
Level 3 Modules
MBB302 Physical Methods for Studying Biological Structures
- Deconvolution of conformational exchange from Raman spectra of aqueous RNA nucleosides. Communications Chemistry, 3(1). View this article in WRRO
- Mapping hidden residual structure within the Myc bHLH-LZ domain using chemical denaturant titration. Structure. View this article in WRRO
- β1 integrin is a sensor of blood flow direction. Journal of Cell Science. View this article in WRRO
- Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-O-methyltransferase. ACS Catalysis, 9(5), 4394-4401.
- 1H, 15N and 13C backbone resonance assignments of the P146A variant of β-phosphoglucomutase from Lactococcus lactis in its substrate-free form. Biomolecular NMR Assignments, 13(2), 349-356.
- Nonequivalence of Second Sphere “Noncatalytic” Residues in Pentaerythritol Tetranitrate Reductase in Relation to Local Dynamics Linked to H-Transfer in Reactions with NADH and NADPH Coenzymes. ACS Catalysis, 8(12), 11589-11599. View this article in WRRO
- van der Waals Contact between Nucleophile and Transferring Phosphorus Is Insufficient To Achieve Enzyme Transition-State Architecture. ACS Catalysis, 8(9), 8140-8153. View this article in WRRO
- Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1. Nucleic Acids Research, 46(11), 5618-5633. View this article in WRRO
- Myc phosphorylation in its basic helix–loop–helix region destabilizes transient α-helical structures, disrupting Max and DNA binding. Journal of Biological Chemistry, 293(24), 9301-9310. View this article in WRRO
- 1H, 15N and 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2. Biomolecular NMR Assignments, 12(1), 79-83. View this article in WRRO
- ¹H, ¹⁵N, ¹³C backbone resonance assignments of human phosphoglycerate kinase in a transition state analogue complex with ADP, 3-phosphoglycerate and magnesium trifluoride.. Biomolecular NMR Assignments, 11(2), 251-256. View this article in WRRO
- Assessing the Influence of Mutation on GTPase Transition States by Using X‐ray Crystallography, 19F NMR, and DFT Approaches. Angewandte Chemie, 129(33), 9864-9867. View this article in WRRO
- Assessing the Influence of Mutation on GTPase Transition States by Using X‐ray Crystallography, 19F NMR, and DFT Approaches. Angewandte Chemie International Edition, 56(33), 9732-9735. View this article in WRRO
- How to name atoms in phosphates, polyphosphates, their derivatives and mimics, and transition state analogues for enzyme-catalysed phosphoryl transfer reactions (IUPAC Recommendations 2016). Pure and Applied Chemistry, 89(5), 653-675. View this article in WRRO
- Metallfluoride als Analoga für Studien an Phosphoryltransferenzymen. Angewandte Chemie, 129(15), 4172-4192.
- Metal Fluorides as Analogues for Studies on Phosphoryl Transfer Enzymes. Angewandte Chemie International Edition, 56(15), 4110-4128. View this article in WRRO
- 1H, 15N, 13C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol. Biomolecular NMR Assignments. View this article in WRRO
- 19F NMR and DFT Analysis Reveal Structural and Electronic Transition State Features for RhoA-Catalyzed GTP Hydrolysis. Angewandte Chemie, 128(10), 3379-3383.
- 19 F NMR and DFT Analysis Reveal Structural and Electronic Transition State Features for RhoA-Catalyzed GTP Hydrolysis. Angewandte Chemie International Edition, 55(10), 3318-3322. View this article in WRRO
- Metal Ion-dependent Heavy Chain Transfer Activity of TSG-6 Mediates Assembly of the Cumulus-Oocyte Matrix. Journal of Biological Chemistry, 290(48), 28708-28723. View this article in WRRO
- Limited Proteolysis Reveals That Amyloids from the 3D Domain-Swapping Cystatin B Have a Non-Native β-Sheet Topology. Journal of Molecular Biology, 427(15), 2418-2434.
- Real-time pure shift 15N HSQC of proteins: a real improvement in resolution and sensitivity. Journal of Biomolecular NMR, 62(1), 43-52. View this article in WRRO
- N-terminal Domain of Prion Protein Directs Its Oligomeric Association. Journal of Biological Chemistry, 289(37), 25497-25508. View this article in WRRO
- α-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction. Proceedings of the National Academy of Sciences, 111(34), 12384-12389.
- P2-067: IMMUNOGLOBULIN-GENERAL AMYLOID INTERACTION MOTIF (IG-GAIM) MOLECULES TARGET BETA AMYLOID AND NEUROFIBRILLARY TANGLES IN VITRO AND IN VIVO. Alzheimer's & Dementia, 10, P494-P494.
- A Bacteriophage Capsid Protein Provides a General Amyloid Interaction Motif (GAIM) That Binds and Remodels Misfolded Protein Assemblies. Journal of Molecular Biology.
- Simultaneously Enhancing Spectral Resolution and Sensitivity in Heteronuclear Correlation NMR Spectroscopy. Angewandte Chemie, 125(44), 11830-11833.
- Simultaneously enhancing spectral resolution and sensitivity in heteronuclear correlation NMR spectroscopy.. Angew Chem Int Ed Engl, 52(44), 11616-11619. View this article in WRRO
- P2-050: A novel mechanism that targets misfolded protein assemblies. Alzheimer's & Dementia, 9, P361-P362.
- Fast protein motions are coupled to enzyme H-transfer reactions.. J Am Chem Soc, 135(7), 2512-2517.
- Charge-Balanced Metal Fluoride Complexes for Protein Kinase A with Adenosine Diphosphate and Substrate Peptide SP20. Angewandte Chemie, 124(49), 12408-12411.
- Measurement of energy landscape roughness of folded and unfolded proteins.. Proc Natl Acad Sci U S A, 109(48), 19563-19568.
- Charge-balanced metal fluoride complexes for protein kinase A with adenosine diphosphate and substrate peptide SP20.. Angew Chem Int Ed Engl, 51(49), 12242-12245.
- Mapping local structural perturbations in the native state of stefin B (cystatin B) under amyloid forming conditions. Frontiers in Molecular Neuroscience(AUG 2012), 1-30. View this article in WRRO
- Reflections on biocatalysis involving phosphorus. BIOCHEMISTRY-MOSCOW, 77(10), 1083-1096.
- Direct Evidence of Generation and Accumulation of β-Sheet-rich Prion Protein in Scrapie-infected Neuroblastoma Cells with Human IgG1 Antibody Specific for β-Form Prion Protein. Journal of Biological Chemistry, 287(17), 14023-14039.
- Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.. Proc Natl Acad Sci U S A, 109(18), 6910-6915.
- Non-toxic Salvia sclareoides Brot. extracts as a source of functional food ingredients: Phenolic profile, antioxidant activity and prion binding properties. Food Chemistry.
- Non-toxic Salvia sclareoides Brot. extracts as a source of functional food ingredients: Phenolic profile, antioxidant activity and prion binding properties. Food Chemistry, 132(4), 1930-1935.
- Versatile low-molecular-weight hydrogelators: achieving multiresponsiveness through a modular design.. Chemistry, 17(35), 9753-9761.
- Modulation of contact order effects in the two-state folding of stefins A and B.. Biophys J, 100(9), 2268-2274.
- Prioritization of charge over geometry in transition state analogues of a dual specificity protein kinase.. J Am Chem Soc, 133(11), 3989-3994.
- Pharmacological chaperone for the structured domain of human prion protein.. Proc Natl Acad Sci U S A, 107(41), 17610-17615.
- The H187R mutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like form.. Biochemistry, 49(40), 8729-8738.
- A Pharmacological Chaperone for the Structured Domain of Human Prion Protein. PRION, 4(3), 130-130.
- Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis.. J Am Chem Soc, 132(18), 6507-6516.
- Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes.. Proc Natl Acad Sci U S A, 107(10), 4555-4560.
- Structural tightening and interdomain communication in the catalytic cycle of phosphoglycerate kinase.. J Mol Biol, 396(2), 345-360.
- Why did Nature select phosphate for its dominant roles in biology?. NEW J CHEM, 34(5), 784-794.
- MgF(3)(-) and alpha-galactose 1-phosphate in the active site of beta-phosphoglucomutase form a transition state analogue of phosphoryl transfer.. J Am Chem Soc, 131(45), 16334-16335.
- Conformational properties of beta-PrP.. J Biol Chem, 284(33), 21981-21990.
- Cryogenic and laser photoexcitation studies identify multiple roles for active site residues in the light-driven enzyme protochlorophyllide oxidoreductase.. J Biol Chem, 284(27), 18160-18166.
- Folding kinetics of the human prion protein probed by temperature jump.. Proc Natl Acad Sci U S A, 106(14), 5651-5656.
- Kinetic analysis of beta-phosphoglucomutase and its inhibition by magnesium fluoride.. J Am Chem Soc, 131(4), 1575-1588.
- The mechanism of amyloid-fibril formation by stefin B: temperature and protein concentration dependence of the rates.. Proteins, 74(2), 425-436.
- The denatured state of N-PGK is compact and predominantly disordered.. J Mol Biol, 385(1), 266-277. View this article in WRRO
- A method for the reversible trapping of proteins in non-native conformations.. Biochemistry, 47(51), 13620-13634.
- A pulse--radiolysis approach to fast reductive cleavage of a disulfide bond to uncage enzyme activity.. Free Radic Biol Med, 45(9), 1271-1278.
- Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes.. J Am Chem Soc, 130(12), 3952-3958.
- Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein.. J Mol Biol, 375(2), 487-498.
- Essential role of proline isomerization in stefin B tetramer formation.. J Mol Biol, 366(5), 1569-1579.
- Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4.. Biochem J, 400(3), 501-510.
- A thiol labelling competition experiment as a probe for sidechain packing in the kinetic folding intermediate of N-PGK.. J Mol Biol, 364(4), 810-823.
- A reassessment of copper(II) binding in the full-length prion protein.. Biochem J, 399(3), 435-444.
- A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site.. Proc Natl Acad Sci U S A, 103(40), 14732-14737.
- Evidence supporting a cis-enediol-based mechanism for Pyrococcus furiosus phosphoglucose isomerase.. J Mol Biol, 358(5), 1353-1366.
- The denatured state under native conditions: a non-native-like collapsed state of N-PGK.. J Mol Biol, 357(2), 365-372.
- Folding and amyloid-fibril formation for a series of human stefins' chimeras: any correlation?. Proteins, 62(4), 918-927.
- Structure and dynamics of coxsackievirus B4 2A proteinase, an enyzme involved in the etiology of heart disease.. J Virol, 80(3), 1451-1462.
- Amplification of bifunctional ligands for calmodulin from a dynamic combinatorial library.. Chemistry, 12(4), 1081-1087.
- Definable equilibrium states in the folding of human prion protein.. Biochemistry, 44(50), 16649-16657.
- Obligate heterodimerization of the archaeal Alba2 protein with Alba1 provides a mechanism for control of DNA packaging.. Structure, 13(7), 963-971.
- Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.. Structure, 13(4), 609-616.
- Determinants of the endosomal localization of sorting nexin 1.. Mol Biol Cell, 16(4), 2049-2057.
- Enhanced ligand affinity for receptors in which components of the binding site are independently mobile.. Chem Biol, 12(1), 89-97.
- The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC.. J Biol Chem, 279(27), 28515-28521.
- Synthesis and photochemistry of a new class of photocleavable protein cross-linking reagents.. Chemistry, 10(7), 1705-1710.
- Comparison of backbone dynamics of monomeric and domain-swapped stefin A.. Proteins, 54(3), 500-512.
- Beyond the EX1 limit: probing the structure of high-energy states in protein unfolding.. J Mol Biol, 336(2), 497-508.
- Cystatin forms a tetramer through structural rearrangement of domain-swapped dimers prior to amyloidogenesis.. J Mol Biol, 336(1), 165-178.
- Effects of domain dissection on the folding and stability of the 43 kDa protein PGK probed by NMR.. J Mol Biol, 330(5), 1189-1201.
- Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P.. J Biol Chem, 278(17), 15304-15312.
- Quaternary structure built from subunits combining NMR and small-angle x-ray scattering data.. Biophys J, 83(2), 1177-1183.
- Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate state.. Biochem Soc Trans, 30(4), 543-547.
- Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily.. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 223, C36-C36.
- Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily.. EMBO J, 20(17), 4774-4781.
- Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones.. Nat Struct Biol, 8(8), 701-704.
- Location and properties of metal-binding sites on the human prion protein.. Proc Natl Acad Sci U S A, 98(15), 8531-8535.
- A rational approach to identifying treatments for prion diseases. FUNDAMENTAL & CLINICAL PHARMACOLOGY, 15, 112-112.
- Wild-type and met-65-->Leu variants of human cystatin A are functionally and structurally identical.. Biochemistry, 39(51), 15783-15790.
- Computer-assisted structure determination. Structure Of the peptide moroidin from laportea moroides. J Org Chem, 65(24), 8406.
- The major transition state in folding need not involve the immobilization of side chains.. Proc Natl Acad Sci U S A, 97(11), 5790-5795.
- Molecular studies of prion propagation. Neurobiology of Aging, 21, 209-209.
- Erratum: Computer-assisted structure determination. Structure of the peptide moroidin from Laportea moroides (Journal of Organic Chemistry (1989) 54 (1901)). Journal of Organic Chemistry, 65(24), 8406-8406.
- Letter to the Editor: Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated protein p23(fyp) from Schizosaccharomyces pombe. J BIOMOL NMR, 16(1), 83-84.
- Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated protein p23fyp from Schizosaccharomyces pombe.. J Biomol NMR, 16(1), 83-84.
- Structural mobility of the human prion protein probed by backbone hydrogen exchange.. Nat Struct Biol, 6(8), 740-743.
- Differences in the effects of TFE on the folding pathways of human stefins A and B.. Proteins, 36(2), 205-216.
- Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1alpha, MIP-1beta, and RANTES. Characterization of active disaggregated chemokine variants.. J Biol Chem, 274(23), 16077-16084.
- Multiple folding pathways for heterologously expressed human prion protein.. Biochim Biophys Acta, 1431(1), 1-13.
- Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations.. Science, 283(5409), 1935-1937.
- Mechanism-based inhibition of C5-cytosine DNA methyltransferases by 2-H pyrimidinone.. J Mol Biol, 286(2), 389-401.
- Characterisation of low free-energy excited states of folded proteins.. J Mol Biol, 284(5), 1625-1639.
- On the mechanism of human stefin B folding: I. Comparison to homologous stefin A. Influence of pH and trifluoroethanol on the fast and slow folding phases.. Proteins, 32(3), 296-303.
- On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate states.. Proteins, 32(3), 304-313.
- The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L.. Biochemistry, 37(20), 7551-7560.
- Topology, sequence evolution and folding dynamics of an immunoglobulin domain.. Nat Struct Biol, 5(3), 194-198.
- Structure of a kinetic protein folding intermediate by equilibrium amide exchange.. Nat Struct Biol, 4(10), 801-804.
- Protein folding pathways and intermediates. CURR OPIN BIOTECH, 8(4), 400-410.
- Protein folding and intermediates.. Curr Opin Biotechnol, 8(4), 400-410.
- Double and triple resonance NMR methods for protein assignment., 60, 29-52.
- Is the structure of the N-domain of phosphoglycerate kinase affected by isolation from the intact molecule?. Biochemistry, 36(2), 333-340.
- Double and triple resonance NMR methods for protein assignment.. Methods Mol Biol, 60, 29-52.
- Domain behavior during the folding of a thermostable phosphoglycerate kinase.. Biochemistry, 35(49), 15740-15752.
- Complexes formed between calmodulin and the antagonists J-8 and TFP in solution.. Biochemistry, 35(32), 10287-10299.
- Determinants of DNA-binding specificity of ETS-domain transcription factors.. Mol Cell Biol, 16(7), 3338-3349.
- Calcium-induced structural changes and domain autonomy in calmodulin.. Nat Struct Biol, 2(9), 777-783.
- ASYMMETRY IN THE STRUCTURE OF GLYCOPEPTIDE ANTIBIOTIC DIMERS - NMR-STUDIES OF THE RISTOCETIN-A COMPLEX WITH A BACTERIAL-CELL WALL ANALOG. J AM CHEM SOC, 117(30), 7958-7964.
- THE BINDING OF A HYDROPHOBIC DRUG TO THE C-TERMINAL DOMAIN OF CALMODULIN. J CELL BIOCHEM, 70-70.
- THE REFINED SOLUTION STRUCTURE OF HUMAN STEFIN-A. J CELL BIOCHEM, 40-40.
- Characterization of the Elk-1 ETS DNA-binding domain.. J Biol Chem, 270(11), 5805-5811.
- The three-dimensional solution structure of human stefin A.. J Mol Biol, 246(2), 331-343.
- THE ACTION OF TIME-DOMAIN CONVOLUTION FILTERS FOR SOLVENT SUPPRESSION. J MAGN RESON SER B, 106(1), 40-46.
- The DNA recognition subunit of a DNA methyltransferase is predominantly a molten globule in the absence of DNA.. FEBS Lett, 355(1), 57-60.
- MOLECULAR ZIPPERS. J AM CHEM SOC, 116(22), 10292-10293.
- Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinases.. Eur J Biochem, 225(3), 1181-1194.
- Component analysis and characterization of a nuclear deoxyribonucleotidase.. Biochem J, 298 Pt 3, 727-732.
- FOLDING PATHWAY OF APOMYOGLOBIN. ABSTR PAP AM CHEM S, 206, 107-PHYS.
- PRACTICAL ASPECTS OF RECORDING MULTIDIMENSIONAL NMR-SPECTRA IN WATER WITH FLAT BASE-LINES. J MAGN RESON SER A, 103(3), 338-348.
- Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin.. Biochemistry, 32(25), 6337-6347.
- Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal.. Biochemistry, 32(25), 6348-6355.
- Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin.. Biochemistry, 32(25), 6356-6364.
- STRUCTURE DETERMINATION OF HUMAN ELAFIN. J CELL BIOCHEM, 286-286.
- PEPTIDE STRUCTURE FROM NMR. CHEM SOC REV, 21(4), 227-236.
- IMPROVED EXPERIMENTS FOR THE ASSIGNMENT OF CROWDED PEPTIDE SPECTRA. J MAGN RESON, 100(3), 593-597.
- Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin.. J Mol Biol, 226(3), 795-817.
- Preparation of phenylalanine-deuterated, and totally 15N-enriched, calmodulins from Trypanosoma brucei, and its application to drug binding studies.. Biochem Soc Trans, 19(4), 430S.
- THE NATURAL DESIGN OF VANCOMYCIN FAMILY ANTIBIOTICS TO BIND THEIR TARGET PEPTIDES. CIBA F SYMP, 158, 73-91.
- The natural design of vancomycin family antibiotics to bind their target peptides.. Ciba Found Symp, 158, 73-86.
- ChemInform Abstract: Aspects of Molecular Recognition: Solvent Exclusion and Dimerization of the Antibiotic Ristocetin When Bound to a Model Bacterial Cell-Wall Precursor. ChemInform, 20(28).
- Conformation of a T cell stimulating peptide in aqueous solution.. FEBS Lett, 250(2), 400-404.
- COMPUTER-ASSISTED STRUCTURE DETERMINATION - STRUCTURE OF THE PEPTIDE MOROIDIN FROM LAPORTEA-MOROIDES. J ORG CHEM, 54(8), 1901-1904.
- ASPECTS OF MOLECULAR RECOGNITION - SOLVENT EXCLUSION AND DIMERIZATION OF THE ANTIBIOTIC RISTOCETIN WHEN BOUND TO A MODEL BACTERIAL CELL-WALL PRECURSOR. J AM CHEM SOC, 111(7), 2475-2480.
- MOLECULAR-BASIS OF THE ACTIVITY OF ANTIBIOTICS OF THE VANCOMYCIN GROUP. PURE APPL CHEM, 61(3), 585-588.
- ChemInform Abstract: Intramolecular Determinants of Conformation and Mobility Within the Antibiotic Vancomycin. ChemInform, 19(49).
- INTRAMOLECULAR DETERMINANTS OF CONFORMATION AND MOBILITY WITHIN THE ANTIBIOTIC VANCOMYCIN. J AM CHEM SOC, 110(17), 5638-5643.
- ChemInform Abstract: Function of the Amino Sugar and N-Terminal Amino Acid of the Antibiotic Vancomycin in Its Complexation with Cell Wall Peptides.. ChemInform, 19(33).
- ASPECTS OF MOLECULAR RECOGNITION - USE OF A TRUNCATED DRIVEN PSEUDO-NOESY EXPERIMENT TO ELUCIDATE THE ENVIRONMENT OF INTERMOLECULAR ELECTROSTATIC INTERACTIONS IN VANCOMYCIN. J CHEM SOC CHEM COMM(11), 707-709.
- FUNCTION OF THE AMINO SUGAR AND N-TERMINAL AMINO-ACID OF THE ANTIBIOTIC VANCOMYCIN IN ITS COMPLEXATION WITH CELL-WALL PEPTIDES. J AM CHEM SOC, 110(9), 2946-2953.
- Forces in molecular recognition: comparison of experimental data and molecular mechanics calculations.. J Comput Aided Mol Des, 2(1), 31-41.
- Molecular basis of the activity of antibiotics of the vancomycin group.. Biochem Pharmacol, 37(1), 133-141.
- ChemInform Abstract: Structure Elucidation of the Glycopeptide Antibiotic Complex A40926.. ChemInform, 18(52).
- STRUCTURE ELUCIDATION OF THE GLYCOPEPTIDE ANTIBIOTIC COMPLEX A40926. J CHEM SOC PERK T 1(9), 2103-2107.
- SEMISELECTIVE TWO-DIMENSIONAL NMR EXPERIMENTS. J MAGN RESON, 74(2), 386-393.
- ChemInform Abstract: Structure Elucidation of Two Triterpenoid Tetrasaccharides from Androsace saxifragifolia.. Chemischer Informationsdienst, 17(51).
- STRUCTURE ELUCIDATION OF 2 TRITERPENOID TETRASACCHARIDES FROM ANDROSACE-SAXIFRAGIFOLIA. J CHEM SOC PERK T 1(8), 1527-1531.
- The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone. Physical Chemistry Chemical Physics, 17(2), 762-782.
- ChemInform Abstract: Why Did Nature Select Phosphate for Its Dominant Roles in Biology?. ChemInform, 41(34), no-no.
- ChemInform Abstract: Peptide Structure from NMR. ChemInform, 24(12), no-no.
- Isotopically labeled flavoenzymes and their uses in probing reaction mechanisms, Methods in Enzymology (pp. 145-166). Elsevier
- Architecture of the active site and the importance of charge balance in catalysis, Phosphoglycerate Kinase: A Hinge-Bending Enzyme (pp. 203-210).
- THE H-HELIX OF MYOGLOBIN AS A POTENTIAL INDEPENDENT PROTEIN FOLDING DOMAIN, Current Research in Protein Chemistry (pp. 283-293). Elsevier
Conference proceedings papers
- The Catalytic Cycle of hFEN1 Requires Protein and DNA Conformational Changes, but Are They Rate-Limiting?. PROTEIN SCIENCE, Vol. 24 (pp 147-147)
- Extended series of proximal and distal hydrogen bonds underpins RhoA catalyzed GTP hydrolysis via a strain-free transition state. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, Vol. 250
- Kinases, phosphatases, mutases and G-proteins. FEBS JOURNAL, Vol. 280 (pp 93-93)
- Computational studies of intermediate- and transition-state analogs in b-PGM. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, Vol. 245
- Utilization of computed F-19 NMR to identify active site intermediate and transition-state analogs in beta-PGM. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, Vol. 244
- Towards the molecular basis of cumulus matrix formation: structure/function studies on TSG-6. INTERNATIONAL JOURNAL OF EXPERIMENTAL PATHOLOGY, Vol. 91(6) (pp A31-A31)
- Universal Scaling Law for Polypeptide Backbone Dynamics on the Pico- to Millisecond Time Scale. Biophysical Journal, Vol. 96(3) (pp 322a-323a)
- A model for amyloid fibril formation by human stefin B (cystatin B). FEBS JOURNAL, Vol. 275 (pp 199-199)
- FOLDING OF PEPTIDE-FRAGMENTS OF PROTEINS IN WATER SOLUTION. PROTEIN FOLDING : DECIPHERING THE SECOND HALF OF THE GENETIC CODE (pp 95-+)
- FOLDING OF PEPTIDE-FRAGMENTS OF PROTEINS IN AQUEOUS-SOLUTION. FRONTIERS OF NMR IN MOLECULAR BIOLOGY, Vol. 109 (pp 1-13)