Mrs. Brenda Elliott Bowler CRNA
Doctor
2925 DeBarr Rd Anchorage AK, 99508About
Mrs. Brenda Elliott Bowler CRNA is a top Doctor in Anchorage, AK. With a passion for the field and an unwavering commitment to their specialty, Mrs. Brenda Elliott Bowler CRNA is an expert in changing the lives of their patients for the better. Through their designated cause and expertise in the field, Mrs. Brenda Elliott Bowler CRNA is a prime example of a true leader in health care. As a leader and expert in their field, Mrs. Brenda Elliott Bowler CRNA is passionate about enhancing patient quality of life. They embody the values of communication, safety, and trust when dealing directly with patients. In Anchorage, AK, Mrs. Brenda Elliott Bowler CRNA is a true asset to their field and dedicated to the profession of medicine.
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Expert Publications
Data provided by the National Library of Medicine- The magnitude of changes in guanidine-HCl unfolding m-values in the protein, iso-1-cytochrome c, depends upon the substructure containing the mutation.
- Electron spin lattice relaxation rates for S = 12 molecular species in glassy matrices or magnetically dilute solids at temperatures between 10 and 300 K.
- Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c.
- Electron spin-lattice relaxation rates for high-spin Fe(III) complexes in glassy solvents at temperatures between 6 and 298 K.
- Interspin distances in spin-labeled metmyoglobin variants determined by saturation recovery EPR.
- pH dependence of formation of a partially unfolded state of a Lys 73 --> His variant of iso-1-cytochrome c: implications for the alkaline conformational transition of cytochrome c.
- Direct detection of heat and cold denaturation for partial unfolding of a protein.
- Denatured state thermodynamics: residual structure, chain stiffness and scaling factors.
- Modulation of platinum antitumor drug binding to DNA by linked and free intercalators.
- The effects of hydrophilic to hydrophobic surface mutations on the denatured state of iso-1-cytochrome c: investigation of aliphatic residues.
- Characterization of the guanidine hydrochloride-denatured state of iso-1-cytochrome c by infrared spectroscopy.
- Destabilizing effects of replacing a surface lysine of cytochrome c with aromatic amino acids: implications for the denatured state.
- A lysine 73-->histidine variant of yeast iso-1-cytochrome c: evidence for a native-like intermediate in the unfolding pathway and implications for m value effects.
- Thermal denaturation of iso-1-cytochrome c variants: comparison with solvent denaturation.
- A histidine variant of yeast iso-1-cytochrome c that strongly affects the energetics of the denatured state.
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