K. D. Hardman

ORCID: 0000-0003-3536-8027
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Research Areas
  • Glycosylation and Glycoproteins Research
  • Carbohydrate Chemistry and Synthesis
  • Monoclonal and Polyclonal Antibodies Research
  • Photosynthetic Processes and Mechanisms
  • Protein Structure and Dynamics
  • Peptidase Inhibition and Analysis
  • Enzyme Structure and Function
  • ATP Synthase and ATPases Research
  • Biochemical and Structural Characterization
  • Protein purification and stability
  • Lipid Membrane Structure and Behavior
  • Streptococcal Infections and Treatments
  • Hemoglobin structure and function
  • Drug Transport and Resistance Mechanisms
  • Folate and B Vitamins Research
  • Blood groups and transfusion
  • Liquid Crystal Research Advancements
  • Synthesis of Organic Compounds
  • Neonatal Health and Biochemistry
  • Spectroscopy and Quantum Chemical Studies
  • Inorganic and Organometallic Chemistry
  • Protease and Inhibitor Mechanisms
  • Advanced NMR Techniques and Applications
  • Plant-based Medicinal Research
  • Molecular spectroscopy and chirality

University of Leeds
2023-2025

Institute of Structural and Molecular Biology
2024

DuPont (United States)
1997-1998

University of Illinois Urbana-Champaign
1990-1992

University of Toronto
1985-1986

Genex Systems (United States)
1985

IBM Research - Thomas J. Watson Research Center
1981

IBM (United States)
1981

Harvard University
1981

Argonne National Laboratory
1972

We describe here the first in vivo targeting of tumors with a single-chain antigen-binding protein. The molecule, which was constructed and expressed Escherichia coli, is novel recombinant protein composed variable light-chain (VL), amino acid sequence an immunoglobulin tethered to heavy-chain (VH) by designed peptide. show that this protein, derived from DNA regions antitumor monoclonal antibody B6.2, has same vitro properties as B6.2 Fab' fragment. Comparative pharmacokinetic studies...

10.1093/jnci/82.14.1191 article EN JNCI Journal of the National Cancer Institute 1990-07-18

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXT1.67-.ANG. X-ray structure of the B2 immunoglobulin-binding domain streptococcal protein G and comparison to NMR B1 domainAniruddha Achari, Stephen P. Hale, Andrew J. Howard, G. Marius Clore, Angela M. Gronenborn, Karl D. Hardman, Marc WhitlowCite this: Biochemistry 1992, 31, 43, 10449–10457Publication Date (Print):November 1, 1992Publication History Published online1 May 2002Published inissue 1 November...

10.1021/bi00158a006 article EN Biochemistry 1992-11-01

The structure of the metalloenzyme carboxypeptidase A (peptidyl-L-amino-acid hydrolase, EC 3.4.17.1) has been refined at 1.75 by a restrained least-squares procedure to conventional crystallographic R factor 0.162. Significant results relative catalytic mechanism are described. In native enzyme, zinc coordination number is five (two imidazole N delta 1 nitrogens, two carboxylate oxygens glutamate-72, and water molecule). complex (at 2.0-A resolution) with dipeptide glycyl-L-tyrosine,...

10.1073/pnas.78.6.3408 article EN Proceedings of the National Academy of Sciences 1981-06-01

<title>Abstract</title> SbmA is a membrane transporter from <italic>Escherichia coli</italic> that imports antimicrobial peptides. Although the protein secondary energized by proton gradient, it structurally related to transmembrane domain (TMD) of ATP-binding cassette (ABC) transporters. therefore bridges structural divide between primary and However, remained unclear, if also shares mechanism alternating access with ABC transporters, because only single (outward-open) state has been...

10.21203/rs.3.rs-5827499/v1 preprint EN cc-by Research Square (Research Square) 2025-02-03

Single-chain antibody of the (NH2) VL-linker-VH (COOH) design, was constructed based on prototype high affinity anti-fluorescein monoclonal (mAb) 4-4-20. Purified single-chain (SCA) 4-4-20/212 studied relative to Ig mAb 4-4-20 in terms ligand binding, kinetics, idiotypy, metatypy, and stability denaturing agents. Ligand-binding data correlated with metatypic relatedness liganded site. Anti-metatypic reagents reacted preferentially conformer active site were unreactive free non-liganded...

10.1016/s0021-9258(17)44796-x article EN cc-by Journal of Biological Chemistry 1990-10-01

Despite progress in defining the nature of major histocompatibility complex products that are recognized by T-cell antigen receptor, binding properties and structure receptor have not been solved. The primary problem has difficulty obtaining sufficient quantities active receptor. In this report we show a single-chain gene can be expressed Escherichia coli. protein consists variable (V) regions alpha beta chains (V V beta) encoded cytotoxic T-lymphocyte clone 2C (a H-2b anti-H-2d alloreactive...

10.1073/pnas.89.10.4759 article EN Proceedings of the National Academy of Sciences 1992-05-15

Abstract A molecular model for the complex formed between jack bean lectin concanavalin (Con A) and glycopeptides of biantennary class is described. The was derived using coordinates Con determined by x‐ray crystalographic refinement techniques, with 1.75‐Å resolution data, obtained from 1 H‐nmr measurements, nuclear Overhauser effect. Previous solution crystallographic studies provided several constraints on possible mode interaction glycopeptide. Examination suggests that glycopeptide...

10.1002/bip.360240106 article EN Biopolymers 1985-01-01

Abstract Carboxamidomethyl derivatives of sperm whale metmyoglobin were prepared by reaction at pH 6.8 with iodoacetamide. The modified protein is similar to previously studied carboxymethyl preparations and shows many the properties native, unmodified protein. Preparations obtained compositions in following ranges, expressed as moles histidine derivative per mole protein: 4.8 7.5; dicarboxamidomethylhistidine, 1.6 4.6; 1-carboxamidomethylhistidine, trace 0.5; 3-carboxamidomethylhistidine,...

10.1016/s0021-9258(18)96316-7 article EN cc-by Journal of Biological Chemistry 1967-01-01

Concanavalin A (Con A), a lectin from the jack bean, Canavalia ensiformis, has number of unusual properties which promote interest in its three-dimensional structure. More than 50 years ago while working with urease same source, Sumner studied some other proteins present and thereby isolated, crystallized named Con (Sumner, 1919). It agglutinates erythrocytes various animal species, yeast cells, bacteria starch granules (Sumner Howell, 1936a). since been shown to precipitate certain...

10.1101/sqb.1972.036.01.036 article EN Cold Spring Harbor Symposia on Quantitative Biology 1972-01-01

To survive, all organisms must detect and respond to mechanical cues in their environment. Cells are subjected a plethora of forces, such as hydrostatic pressure, cell-cell contact, stretch, compression, shear stress. Mechanosensitive membrane proteins have evolved across life kingdoms sense forces the membrane. Bacterial mechanosensitive ion channels provide blueprint for understanding fundamental mechanisms that underpin cellular responses signals. Recently, identification eukaryotic force...

10.1016/j.cophys.2023.100689 article EN cc-by Current Opinion in Physiology 2023-06-01

Membrane-bound pyrophosphatases (mPPases) are homodimeric proteins that hydrolyse pyrophosphate and pump H + /Na across membranes. They crucial for the virulence of protist pathogens, making them attractive drug targets. In this study, we investigate inhibitory effects seven distinct bisphosphonates against Thermotoga maritima mPPase to explore their mode action assist in future small molecule inhibitor development. We solved two structures bound inhibitors enzyme active sites probed...

10.7554/elife.102288 preprint EN 2024-12-04

A serum IgG immunoglobulin and a urinary λ type Bence-Jones protein from single patient (Mcg) with multiple myeloma have been crystallized in forms suitable for X-ray diffraction studies (Schiffer et al., 1970; Edmundson 1970b).

10.1101/sqb.1972.036.01.055 article EN Cold Spring Harbor Symposia on Quantitative Biology 1972-01-01

Abstract Membrane-bound pyrophosphatases (mPPases) are homodimeric proteins that hydrolyse pyrophosphate and pump H + /Na across membranes. They crucial for the virulence of protist pathogens, making them attractive drug targets. In this study, we investigate inhibitory effects seven distinct bisphosphonates against Thermotoga maritima mPPase to explore their mode action assist in future small molecule inhibitor development. We solved two structures bound inhibitors enzyme active sites...

10.1101/2024.07.26.605302 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2024-07-26

Membrane-bound pyrophosphatases (mPPases) are homodimeric proteins that hydrolyse pyrophosphate and pump H + /Na across membranes. They crucial for the virulence of protist pathogens, making them attractive drug targets. In this study, we investigate inhibitory effects seven distinct bisphosphonates against Thermotoga maritima mPPase to explore their mode action assist in future small molecule inhibitor development. We solved two structures bound inhibitors enzyme active sites probed...

10.7554/elife.102288.1 preprint EN 2024-12-04

Abstract ChemInform is a weekly Abstracting Service, delivering concise information at glance that was extracted from about 100 leading journals. To access of an article which published elsewhere, please select “Full Text” option. The original trackable via the “References”

10.1002/chin.199746199 article EN ChemInform 1997-11-11

Abstract ChemInform is a weekly Abstracting Service, delivering concise information at glance that was extracted from about 100 leading journals. To access of an article which published elsewhere, please select “Full Text” option. The original trackable via the “References”

10.1002/chin.199830289 article EN ChemInform 1998-07-28

Horse spleen apoferritin,the protein component of the iron-storage ferritin, crystallizes in space

10.1107/s0108767381099133 article EN Acta Crystallographica Section A Foundations of Crystallography 1981-08-16

We have designed a series of benzoic acid derivatives to fit into the active site influenza virus neuraminidase and inhibit its enzymatic activity.Because residues in are conserved for all known strains virus, these types inhibitors potential be highly effective drugs against virus.One such compound, 3,5-diguanidino-4-(N-acetylamino )benzoic (1), shows measurable inhibition activity assays.We solved X-ray crystal stmcture B/Lee/40 complexed with 1 at -l80°C 2.2A resolution.The inhibitor...

10.1107/s0108767396091027 article EN Acta Crystallographica Section A Foundations of Crystallography 1996-08-08
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