Dr. Thomas William Kirby D.C.
Chiropractor
1330 Lawrence St Port Townsend WA, 98368About
Dr. Thomas Kirby is a Chiropractor practicing in Port Townsend, WA. Dr. Kirby specializes in preventing, diagnosing, and treating conditions associated with the neuromusculoskeletal system, while improving each patients functionality and quality of life. Conditions treated include sciatica, neck pain, and arthritis pain, among many others. Dr. Kirby seeks to reduce pain and discomfort through manipulation and adjustment of the spine.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- The nuclease A inhibitor represents a new variation of the rare PR-1 fold.
- Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium.
- Metabolic transformation of AZTp4A by Ap4A hydrolase regenerates AZT triphosphate.
- Solution structure of the lyase domain of human DNA polymerase lambda.
- NMR assignment of protein side chains using residue-correlated labeling and NOE spectra.
- Dynamic characterization of a DNA repair enzyme: NMR studies of [methyl-13C]methionine-labeled DNA polymerase beta.
- Backbone dynamics of the RNase H domain of HIV-1 reverse transcriptase.
- Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III.
- Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III theta subunit.
- A thymine isostere in the templating position disrupts assembly of the closed DNA polymerase beta ternary complex.
- NMR determination of lysine pKa values in the Pol lambda lyase domain: mechanistic implications.
- Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex.
- NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solution.
- NMR assignment of polymerase beta labeled with 2H, 13C, and 15N in complex with substrate DNA.
- Metal-induced DNA translocation leads to DNA polymerase conformational activation.
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