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Biomedical subjects

J Finney

Publications and source records attributed to J Finney.

4 recordsLinked to original sources
PubMed1989

Evaluation of hematuria.

Hematuria is an important sign that indicates the presence of a pathologic condition in the genitourinary tract. Causes can be categorized by where in the urinary tract the problem is located--above the kidney, in the kidney or one of its structures, or below the kidney. Another category is false hematuria, such as urine that has been discolored by intake of a certain food or drug. A thorough history, physical examination, and appropriate laboratory studies, followed by more sophisticated diagnostic tests chosen on the basis of the assembled clues, can establish the diagnosis in most cases. Patients rarely have to be hospitalized or undergo invasive procedures for assessment of hematuria.

Female↗
PubMed1988

Inelastic neutron scattering analysis of picosecond internal protein dynamics. Comparison of harmonic theory with experiment.

The experimental inelastic neutron scattering spectrum of a protein, the bovine pancreatic trypsin inhibitor (BPTI), in a powder sample is presented together with the generalized density of states, G(omega), as a function of the frequency, omega, derived from the scattering data. The experimental results are compared with calculations from two different normal mode analyses of BPTI. One of these, based on an improved model, gives a calculated spectrum and density of states in general agreement with those obtained experimentally; the other, based on an earlier model, shows considerable disagreement. The important improvements in the newer normal mode analysis are the explicit treatment of all atoms (non-polar as well as polar hydrogens are included) and a modified truncation scheme for the long-range electrostatic interactions. The fact that the inelastic neutron scattering measurements can distinguish between the two theoretical models makes clear their utility for the analysis of protein dynamics.

Animals↗
PubMed1987

Direct measurement of hydration-related dynamic changes in lysozyme using inelastic neutron scattering spectroscopy.

Inelastic neutron scattering spectroscopy is used to investigate dynamic changes in lysozyme powder at two different low D2O hydrations (0.07g D2O/g protein and 0.20 g D2O/g protein). In the higher hydration sample, the inelastic scattering between 0.8 and 4.0 cm-1 energy transfer is increased and the elastic scattering is decreased. The decreased elastic scattering suggests increased atomic amplitudes of motion and the increased 0.8 to 4.0 cm-1 scattering suggests increased motions in this frequency range. Comparison with normal mode models of lysozyme dynamics shows that the inelastic difference occurs in the frequency region predicted for the lowest frequency, largest amplitude, global modes of the molecular [M. Levitt, C. Sander and P.S. Stern, J. Mol. Biol. 181, 423 (1985). B. Brooks and M. Karplus, Proc. Natl. Acad. Sci (U.S.A) 82, 4995 (1985), R.E. Bruccoleri, M. Karplus and J.A. McCammon, Biopolymers 25 1767 (1986)]. Our results are consistent with a model in which an increased number of low frequency global modes are present in the higher hydrated sample.

Energy Transfer↗