Christopher R. Walters

ORCID: 0000-0003-2938-6034
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About
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Research Areas
  • Enzyme Structure and Function
  • Chemical Synthesis and Analysis
  • Click Chemistry and Applications
  • Heat shock proteins research
  • Monoclonal and Polyclonal Antibodies Research
  • Protein Structure and Dynamics
  • RNA and protein synthesis mechanisms
  • Glycosylation and Glycoproteins Research
  • Biotin and Related Studies
  • Synthesis and Reactivity of Sulfur-Containing Compounds
  • Enzyme Production and Characterization
  • Neonatal Respiratory Health Research
  • Chemical synthesis and alkaloids
  • Microbial Metabolic Engineering and Bioproduction
  • Sulfur-Based Synthesis Techniques
  • Polysaccharides and Plant Cell Walls
  • Drug Transport and Resistance Mechanisms
  • Carbohydrate Chemistry and Synthesis
  • Assisted Reproductive Technology and Twin Pregnancy
  • Radical Photochemical Reactions
  • Protein purification and stability
  • DNA and Nucleic Acid Chemistry
  • Diabetes Treatment and Management
  • Biochemical and Molecular Research
  • Synthesis and Catalytic Reactions

University of Pennsylvania
2015-2023

Philadelphia University
2017-2018

California University of Pennsylvania
2017

University of Nottingham
1997-2007

Newcastle University
2003-2005

University of Sheffield
2003

A mechanistically distinct, Ni/photoredox-catalyzed arylation of unprotected, native thiols (<italic>e.g.</italic>, cysteine residues) is reported – a process initiated through visible light-promoted, hydrogen atom transfer (HAT) event under ambient conditions.

10.1039/c7sc04292b article EN cc-by Chemical Science 2017-11-13

The expression of proteins containing unnatural amino acids through suppression a stop codon can be limited by truncation due to competition with release factors. When the site incorporation is near C-terminus, it may not feasible separate full-length acid protein from truncated form. We report simple, traceless procedure that allows one isolate desired using C-terminal intein fusion.

10.1021/ja5103019 article EN Journal of the American Chemical Society 2015-01-27

Modular glycoside hydrolases that degrade the plant cell wall often contain noncatalytic carbohydrate-binding modules (CBMs) interact with specific polysaccharides within this complex macromolecule. CBMs, by bringing appended catalytic module into intimate and prolonged association substrate, increase rate at which these enzymes are able to hydrolyze glycosidic bonds. Recently, crystal structure of family 15 CBM (CBM15) from Cellvibrio japonicus (formerly Pseudomonas cellulosa) Xyn10C was...

10.1021/bi0347510 article EN Biochemistry 2003-07-18

A combination of labeling techniques enables site-specific installation fluorescent probes for measuring distances within proteins by Förster resonance energy transfer (FRET).

10.1039/c7cc05492k article EN Chemical Communications 2017-01-01

Combinations of thioamide modifications can enhance protein stability or fluorescence quenching.

10.1039/c8cc00104a article EN Chemical Communications 2018-01-01

The recycling of photosynthetically fixed carbon, by the action microbial plant cell wall hydrolases, is integral to one major geochemical cycles and considerable industrial importance. Non-catalytic carbohydrate-binding modules (CBMs) play a key role in this degradative process targeting hydrolytic enzymes their cognate substrate within complex milieu polysaccharides that comprise wall. Family 29 CBMs have, thus far, only been found an extracellular multienzyme wall-degrading from anaerobic...

10.1074/jbc.m501551200 article EN cc-by Journal of Biological Chemistry 2005-03-23

Site-selective incorporation of thioamides into peptides and proteins provides a useful tool for wide range applications. Current methods suffer from low yields as well epimerization. Here, we describe how the use 1,8-diazabicyclo[5.4.0]undec-7-ene (DBU) rather than piperidine in fluorenylmethyloxycarbonyl (Fmoc) deprotection reduces epimerization increases thioamide-containing peptides. Furthermore, demonstrate that DBU avoids byproduct formation when synthesizing containing side-chain thioamides.

10.1055/s-0036-1589027 article EN Synlett 2017-05-19

ABSTRACT To confirm that Mycobacterium tuberculosis chaperonin 10 (Cpn10) is secreted outside the live bacillus, infected macrophages were examined by electron microscopy. This revealed mycobacterial protein accumulates both in wall of bacterium and matrix phagosomes which ingested mycobacteria survive within macrophages. understand structural implications underlying this secretion, a study M . Cpn10 was performed under conditions are generally believed to mimic membrane environment. It...

10.1128/jb.185.14.4256-4267.2003 article EN Journal of Bacteriology 2003-07-01

To compare the application of a non-radioactive in situ hybridisation (ISH) technique with an immunocytochemical for detection human parvovirus B19 formalin fixed, paraffin wax embedded sections macerated fetal tissue.Archived samples liver, lung or kidney from 19 fetuses were investigated using full length digoxigenin labelled DNA probe 5.5 kb; bound was detected anti-digoxigenin (alkaline phosphatase) conjugate and visualised NBT/BCIP. Immunocytochemical performed monoclonal mouse...

10.1136/jcp.50.9.749 article EN Journal of Clinical Pathology 1997-09-01

Abstract The conditions which favor dissociation of oligomeric Mycobacterium tuberculosis chaperonin 10 and the solution structure monomer were studied by analytical ultracentrifugation, size exclusion chromatography, fluorescence, circular dichroism spectroscopies. At neutral pH in absence divalent cations, protein is fully monomeric below approximately a 4.7 μ M concentration. Under these forms completely unfolded partially folded conformers are equilibrium with each other. One conformer...

10.1002/bip.20106 article EN Biopolymers 2004-07-21
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