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Biomedical subjects

R Scholl

Publications and source records attributed to R Scholl.

14 recordsLinked to original sources
PubMed1992

[Acoustic rhinometry: the bat principle of the nose].

All cross-sectional areas of the upper airway can be measured by an acoustic signal using the acoustic reflection technique, or acoustic rhinometry. The plane of the cross-sectional areas measured was determined in nasal models. The isotemporal layers were found to be nearly parallel to the nasal valve. The acoustically measured cross-sectional areas correlated with the cross-sectional areas of cuts from nasal models. After digitizing these cuts, a CAD software calculates cross-sectional areas in all orientations and at all distances. The difference between the measured and calculated cross-sectional areas is up to 3% in the nasal cavity and up to 17% in the nasopharynx. The hypothesis that the cross-sectional areas measured lie nearly parallel to the nasal valve was confirmed. The normal rhinometric curve shows the minimal cross-sectional area (I-notch) to lie at the nasal isthmus. The second narrowest segment of the nasal cavity lies at the head of the inferior concha and septal concha (C-notch). Characteristic examples of patients with turbinate hypertrophy, choanal atresia, enlarged adenoids, and septal deviations are presented. Acoustic rhinometric curves can only be interpreted in combination with the rhinoscopic findings because different pathological conditions can produce similar curves. Recording of reliable and reproducible data by acoustic rhinometry demands that the connection between the rhinometer and the nose does not distort the valve area. When we used two different nose pieces (1.2 and 1.5 cm outer diameter) the cross-sectional areas in the anterior third of the nose of only 28% of the patients was measured correctly.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenoids↗
PubMed1990

Conformational substates and motions in myoglobin. External influences on structure and dynamics.

Myoglobin, a simppe dioxygen-storage protein, is a good laboratory for the investigation of the connection between protein structure, dynamics, and function. Fourier-transform infrared spectroscopy on carbon-monoxymyoglobin (MbCO) shows three major CO bands. These bands are excellent probes for the investigation of the structure-function relationship. They have different CO binding kinetics and their CO dipoles form different angles with respect to the heme normal, implying that MbCO exists in three major conformational substates, A0, A1, and A3. The entropies and enthalpies of these substates depend on temperature above approximately 180 K and are influenced by pH, solvent, and pressure. These results suggest that even a protein as simple as Mb can assume a small number of clearly different structures that perform the same function, but with different rates. Moreover, protein structure and dynamics depend strongly on the interaction of the protein with its environment.

Fourier Analysis↗
PubMed1988

Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine.

Low-temperature flash photolysis with IR and visible spectroscopy was used to probe the influence of the distal histidine His-64(E7) of sperm-whale myoglobin (Mb) on the orientation of bound carbon monoxide (CO) and on the kinetics of CO rebinding. The synthesis and high-level expression of a sperm-whale myoglobin gene in Escherichia coli permits the efficient substitution of the distal histidine through site-directed mutagenesis. Substitution of His-E7 with glycine [GlyE7]Mb bound with CO (CO[GlyE7]Mb) results in one broad bound-CO IR stretch band, v(C-O), centered at 1973 cm-1 at 10 K, in contrast to three distinct bands for native and synthetic wild-type MbCO at 1966, 1945, and 1929 cm-1. After flash photolysis at 10 K, the unbound state of CO[GlyE7]Mb exhibits two CO stretch bands, whereas MbCO has three. Fourier transform IR spectroscopy measurements of the linear dichroism after photoselective flash photolysis of CO bound to [GlyE7]Mb at 10 K reveals the bound CO to be oriented at an angle of alpha = 20 degrees +/- 2 degrees with respect to the heme normal. Flash photolysis data from 10 to 300 K provide evidence for a larger distal pocket and a smaller enthalpy barrier (by approximately 4 kJ/mol) for [GlyE7]MbCO as compared with wild-type MbCO. These results reinforce the notion that the dominant control of the binding step at the heme iron comes from the proximal side through the protein structure.

Animals↗
PubMed1987

[Replacement of the head of the humerus as a rescue operation following dislocated compound fractures of the shoulder joint].

Results after conservative or surgical treatment of comminuted fractures of the head of the humerus are often unsatisfactory and complicated by pain and a severely decreased range of motion. In these patients good results have been obtained by replacement of the humeral head with the Isoelastic Humeral Head Prosthesis. Fourteen cases are reported and their results discussed.

Adult↗