Dr. George W Farr MD
Anesthesiologist
501 20th St Knoxville TN, 37916About
Dr. George Farr is an anesthesiologist practicing in Knoxville, TN. Dr. Farr ensures the safety of patients who are about to undergo surgery. Anestesiologists specialize in general anesthesia, which will (put the patient to sleep), sedation, which will calm the patient or make him or her unaware of the situation, and regional anesthesia, which just numbs a specific part of the body. As an anesthesiologist, Dr. Farr also might help manage pain after an operation.
Education and Training
Univ of Tn, Memphis, Coll of Med, Memphis Tn 1994
Georgetown University in Washington DC 1994
Board Certification
AnesthesiologyAmerican Board of AnesthesiologyABA
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Evidence that beta-tubulin induces a conformation change in the cytosolic chaperonin which stabilizes binding: implications for the mechanism of action.
- Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes.
- Site-directed mutagenesis of the GTP-binding domain of beta-tubulin.
- A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.
- Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
- Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation.
- TCP1 complex is a molecular chaperone in tubulin biogenesis.
- Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.
- GroEL-GroES-mediated protein folding.
- Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.
- Two families of chaperonin: physiology and mechanism.
- Topologies of a substrate protein bound to the chaperonin GroEL.
- Multiple states of a nucleotide-bound group 2 chaperonin.
- Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state.
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