A5103350877- Redox biology and oxidative stress
- Enzyme Structure and Function
- Prion Diseases and Protein Misfolding
- Mass Spectrometry Techniques and Applications
- Protein Structure and Dynamics
- Sulfur Compounds in Biology
- Click Chemistry and Applications
- Computational Drug Discovery Methods
- HIV/AIDS drug development and treatment
- RNA modifications and cancer
- Biochemical and Molecular Research
- RNA Research and Splicing
- Trypanosoma species research and implications
- Inflammatory mediators and NSAID effects
- Spectroscopy and Quantum Chemical Studies
- melanin and skin pigmentation
- Ion-surface interactions and analysis
- Laser Material Processing Techniques
- Trace Elements in Health
- Biochemical Analysis and Sensing Techniques
- Biochemical effects in animals
- RNA and protein synthesis mechanisms
- Advanced machining processes and optimization
- Advanced Physical and Chemical Molecular Interactions
- Skin Protection and Aging
Cranfield University
2020
Wake Forest University
2005-2010
Elizabeth City State University
2005
University of Reading
2005
Cardiff University
2000-2003
Cysteine sulfenic acid formation in proteins results from the oxidative modification of susceptible cysteine residues by hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. This species represents a biologically significant occurring during oxidant signaling or stress, it can modulate protein function. Most methods to identify such oxidatively modified rely on monitoring loss one more thiol group(s) selective labeling nascent groups following reduction oxidized proteins. Our previous...
Cysteine sulfenic acids in proteins can be identified by their ability to form adducts with dimedone, but this reagent imparts no spectral or affinity tag for subsequent analyses of such tagged proteins. Given its similar reactivity toward cysteine acids, 1,3-cyclohexadione was synthetically modified an alcohol derivative and linked fluorophores based on isatoic acid 7-methoxycoumarin. The resulting compounds retain full specificity proteins, allowing incorporation the fluorescent label into...
Abstract Typical 2-Cys peroxiredoxins (Prxs) are peroxidases which regulate cell signaling pathways, apoptosis, and differentiation. These enzymes obligate homodimers, can form decamers in solution. During catalysis, Prxs exhibit cysteine-dependent reactivity requires the deprotonation of peroxidatic cysteine (Cp) supported by a lowered pKa initial step. We present results molecular dynamics simulations combined with calculations on monomeric, dimeric decameric forms one typical Prx,...
Abstract Long‐range functional communication is a hallmark of many enzymes that display allostery, or action‐at‐a‐distance. Many aminoacyl‐tRNA synthetases can be considered allosteric, in their trinucleotide anticodons bind the enzyme at site removed from catalytic domains. Such case with E. coli methionyl‐tRNA synthase (MetRS), which recognizes its cognate anticodon using conserved tryptophan residue 50 Å away tRNA aminoacylation. The lack details regarding how MetRS and Met interact has...
Two novel tyrosinase mediated drug delivery pathways have been investigated for the selective of cytotoxic units to melanocytes from urea and thiourea prodrugs. The synthesis these prodrugs is reported, as well oximetry data that illustrate targets are substrates tyrosinase. stability each in (i) phosphate buffer (ii) bovine serum discussed, identified lead candidates further studies. Finally, HPLC studies preliminary cytotoxicity a melanotic an amelanotic cell line, feasibility approach, presented.
The peroxiredoxins (Prx) are ubiquitous peroxidases involved in important biological processes; however, details of their enzymatic mechanism remain elusive. To probe potential dynamics-function relationships, molecular dynamics simulations and electrostatic calculations were performed on the atypical 2-cysteine thiol peroxidase (Tpx) from Streptococcus pneumoniae results compared to a previous study typical Prx Trypanosoma cruzi. analyses indicate commonality between both Prx: dynamic...
A major pharmaceutical problem is designing diverse and selective lead compounds. The human genome sequence provides opportunities to discover compounds that are protein if we can develop methods identify specificity determinants from alone. We have analyzed structural diversity of sheep COX-1 mouse COX-2 proteins by Active Site Profiling (ASP). Eleven residues should serve as between were identified; however, the literature suggests only one has been utilized in structure-based discovery....
A novel protocol for modelling the unfolding pathway has been developed which focuses on protein–solvent interface. The method is based a cavity search algorithm, PRO-ACT, allows us to locate and define cavities within native protein structures. By comparison with experimental data from X-ray crystallography buried solvent molecules in proteins, we have found that are likely be occupied by larger more polar surface. placing into may not normally fully hydrated then relaxing structure short...