Dr. Chad Robert Matthews D.M.D.
Periodontist | Periodontics
1033 Bayshore Dr Suite A Rock Hill SC, 29732About
Dr. Chad Matthews practices Periodontics in Rock Hill, SC. A periodontist is a dentist who specializes in the prevention, diagnosis, and treatment of periodontal disease, and in the placement of dental implants. Dr. Matthews has expertise in the treatment of oral inflammation and often treats problematic periodontal cases, such as those with severe gum disease or a complex medical history. Some treatments that Dr. Matthews provides are scaling and root planing and root surface debridement.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Analysis of kinetics using a hybrid maximum-entropy/nonlinear-least-squares method: application to protein folding.
- Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: a test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels.
- A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding.
- A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein.
- Parallel channels and rate-limiting steps in complex protein folding reactions: prolyl isomerization and the alpha subunit of Trp synthase, a TIM barrel protein.
- Sequential vs. parallel protein-folding mechanisms: experimental tests for complex folding reactions.
- Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein.
- The coordination of the isomerization of a conserved non-prolyl cis peptide bond with the rate-limiting steps in the folding of dihydrofolate reductase.
- Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase.
- Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein.
- Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1.
- Zinc binding drives the folding and association of the homo-trimeric gamma-carbonic anhydrase from Methanosarcina thermophila.
- An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein.
- Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein.
- Molecular dimensions and their distributions in early folding intermediates.
Dr. Chad Robert Matthews D.M.D.'s Practice location
Practice At 1033 Bayshore Dr Suite A
1033 Bayshore Dr Suite A -Rock Hill, SC 29732Get Direction
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