Dr. Matthew Ryan Groves D.C.
Chiropractor
2100 Jacobssen Dr Normal IL, 61761About
Dr. Matthew Groves is a Chiropractor practicing in Normal, IL. Dr. Groves 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. Groves 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- Topological characteristics of helical repeat proteins.
- Functional characterization of recombinant chloroplast signal recognition particle.
- Definition of domain boundaries and crystallization of the SMN Tudor domain.
- High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues.
- Crystallization of a Golgi-associated PR-1-related protein (GAPR-1) that localizes to lipid-enriched microdomains.
- Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism.
- The impact of protein characterization in structural proteomics.
- Octameric alcohol oxidase dissociates into stable, soluble monomers upon incubation with dimethylsulfoxide.
- A method for the general identification of protein crystals in crystallization
- The assembly of the plasmodial PLP synthase complex follows a defined course.
- Crystallization and preliminary characterization of a novel haem-binding protein of Streptomyces reticuli.
- Methods for protein characterization by mass spectrometry, thermal shift (ThermoFluor) assay, and multiangle or static light scattering.
- The oligomeric assembly of the novel haem-degrading protein HbpS is essential for interaction with its cognate two-component sensor kinase.
- The three-component signalling system HbpS-SenS-SenR as an example of a redox sensing pathway in bacteria.
- Mobility of the conserved glycine 155 is required for formation of the active plasmodial Pdx1 dodecamer.
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