Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Optical Rotatory Dispersion”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,711 records · Page 95Linked to original sources
PubMed1970

Temporal resolution of individual steps in an enzymic reaction at low temperature.

Media are described which make it possible to study mechanisms of enzyme action at low temperature. The applicability of techniques developed are illustrated by results obtained on formation kinetics of complexes produced by the interaction of horseradish peroxidase with hydrogen peroxide. It is shown that the various steps in the time course of the reaction can be readily resolved with isolation of each intermediate in concentrations sufficient to permit rate studies between consecutive steps. The potential of the method for elaboration of enzyme mechanisms is discussed.

Chemical Phenomena↗
PubMed1970

Optical activity of biological membranes: scattering effects and protein conformation.

THE FOLLOWING QUESTION HAS RECENTLY ARISEN IN THE LITERATURE CONCERNING THE INTERPRETATION OF THE OPTICAL ACTIVITY OF BIOLOGICAL MEMBRANES: do the characteristic spectral distortions observed for diverse membrane systems reflect some common and unique aspect of membrane architecture or are they the result of scattering effects owing to the particulate nature of membranous systems? We have confirmed the latter interpretation on the basis of the following experimental observations: (a) red blood cell membranes give a normal circular dichroism spectrum when scattering is reduced and (b) nonaggregated, nonmembranous helical proteins give distorted membranelike spectra when scattering is introduced. An improved estimate of secondary structure on the basis of undistorted spectra results in about 50 per cent alpha-helix for red blood cell membrane protein. In addition we conclude that the distortions in optical activity spectra offer no evidence in support of various proposed membrane models.

Circular Dichroism↗
PubMed1970

Conformational similarity of ovine prolactin and bovine growth hormone.

The behavior and properties of ovine prolactin have been evaluated by measurements of fluorescence, polarization of fluorescence, absorption, optical rotation, and circular dichroism. The helical content of the native molecule at pH 8 is 60 per cent as determined by circular dichroism. Three molecular transitions have been followed. The one in acid affects only 20 per cent of the helical residues. More profound conformational changes occur in urea solutions (pH 5.2 and 8.0) where most of the helical residues are randomized. There is a close parallel between the behavior of ovine prolactin and bovine growth hormone both in aqueous solutions between pH 2 and 11.5 and in urea solutions at pH 5.2 and 8.0. Based on the similarities in behavior it is proposed that the conformations of these two hormones are homologous.

Animals↗
PubMed1970

Circular dichroism studies at variable temperature: urobilinoid conformation.

Measurements of the temperature dependence of the circular dichroism spectra of l-stercobilin and d-urobilin show that the conformations of these optically-active urobilinoids change with temperature between 163 and 297 degrees K. These conformational changes depend critically on the hydrogen bonding characteristics of the solvent. Thus, in methanol-glycerol (9:1), the chiral sense of the helical conformation of the dipyrrylmethene chromophore is reversed on lowering the temperature, whereas in chloroform, reversal does not occur.

Bile Pigments↗
PubMed1971

Absolute configuration of Cecropia juvenile hormone.

The absolute configuration of the predominant Cecropia hormone, methyl 12,14-dihomojuvenate, has been determined to be methyl (E,E)-(10R,11S)-(+)-10,11-epoxy-7-ethyl-3,11-dimethyl-2, 6-tridecadienoate (I). The less abundant hormone, methyl 12-homojuvenate, can be presumed by analogy to have the corresponding 3,7,11-trimethyldienoate structure (II). The assignment has been established with microamounts of substance by applying Horeau's method to the glycol derivative (III) of the hormone.The course of the perchloric acid-catalyzed epoxide ring opening of I was checked by conducting the conversion in (18)O-labeled water. It has been ascertained that the configuration at the secondary hydroxyl group of the resulting III remained unchanged. On the other hand, the hydration proceeded with a surprisingly high rate of cis opening.

Animals↗
PubMed1973

Circular dichrosim of chromaffin granule proteins in situ: analysis of turbidity effects and protein conformation.

The circular dichroism spectra for proteins in situ in catecholamine secretory vesicles (chromaffin granules) is presented together with an analysis of protein conformation and turbidity effects on the spectra. The calculational analysis has resolved scattering and absorption effects in the turbid suspension spectra using a coated-sphere scattering model which allows for different materials in its shell and core. The intrinsic conformation of the proteins in situ was estimated by an iterative procedure with various trial protein conformations, for the chromaffin granules both intact and after release of their contents. The resulting average secondary structures (within about 10%) are: (25% alpha helix, 15% beta structure) for the membrane proteins and (15% alpha helix, 5% beta structure) for the soluble contents. The protein conformation did not change with osmotic release of the granule's contents. Consequently, if chromogranins are involved in a catecholamine storage complex, this is not reflected in any detectable change in their average secondary structure.

Cell Fractionation↗
PubMed1974

Effect of alkylureas on the polymerization of hemoglobin S.

Alkylureas (methyl-, ethyl-, propyl-, and butyl-) can inhibit both the gelation of deoxyhemoglobin S and red cell sickling without denaturation of the hemoglobin or intrinsic alteration of its oxygen affinity. This effect is directly proportional to the length of the alkyl chain and substantiates the importance of hydrophobic interactions in the polymerization of hemoglobin S. In addition, it opens the possibility that further systematic investigations with these compounds will help quantitate the role of hydrophobic interactions in this system so as to further our understanding of the polymerization of deoxyhemoglobin S.

Chemical Phenomena↗
PubMed1998

Organization of HIV-1 capsid proteins on a lipid monolayer.

In an in vitro system that mimics the assembly of immature human immunodeficiency virus (HIV) particles, ordered arrays of HIV-1 capsid (CA) proteins encoded by the viral gag gene have been obtained by incubation of histidine-tagged capsid proteins (His-HIVCA) beneath lipid monolayers containing the nickel-chelating lipid, 1,2-di-O-hexadecyl-sn-glycero-3-(1'-2"-R-hydroxy-3'-N-(5-amino-1- carboxypentyl)iminodiacetic acid)propyl ether. The membrane-bound His-HIVCA proteins formed small crystalline arrays of primitive (p1) unit cells with dimensions of a = 74.2 A, b = 126.2 A, gamma = 89.3 degrees. The image-analyzed two-dimensional projection of His-HIVCA assemblies shows a cage-like lattice, consisting of hexamer and trimer units, surrounding protein-free cage holes. The hexamer-coordinated cage holes of 26.3-A diameter are spaced at 74. 2-A intervals: these distances, and the hexamer-trimer arrangement, are consistent with previous, lower resolution studies on immature HIV-1 virus particles produced in vivo. Additionally, HIV-1 matrix protein trimer unit structures align to the His-HIVCA trimer units such that residues previously shown to interact with the HIV-1 gp120/gp41 envelope protein complex are oriented toward the hexamer cage holes. Our results form a bridge between results from conventional methods for the analysis of HIV particle structure.

Capsid↗
PubMed1989

SED88: a Pascal program for the analysis of sedimentation equilibrium data.

Analytical ultracentrifugation is commonly used for the determination of molecular weights (sedimentation equilibrium) and sedimentation coefficients (sedimentation rate) of biological macromolecules in solution. A Turbo Pascal program for the analysis of sedimentation equilibrium centrifugation data produced by absorbance optical systems is described. The user may enter data from a scan of absorbance versus distance from the centre of rotation, via a graphics tablet (or ASCII file). This is subsequently manipulated to yield an apparent weight average molecular weight for the given sample. Plots of ln (absorbance) versus (radius2) may also be produced. The method described uses readily available computational equipment requiring only a graphics tablet in addition to an IBM PC compatible computer. This technique and the software developed have been used to investigate the molecular weight range of two International Humic Substances Society (IHSS) reference samples from the Suwannee River.

Absorption↗
PubMed1975

The use of s-2-cyanoethyl phosphorothioate in the preparation of oligo 5'-deoxy-5'-thiothymidylates.

An improvement of our strategy for the stepwise synthesis of oligo 5'-deoxy-5'-thiodeoxyribonucleotides [Chladek and Nagyvary (1972) J. Amer. Chem. Soc. 94, 2079] involves the use of 5'-O-tosylthymidine 3'-S-2-cyanoethyl phosphorothioate. The displacement of the tosylate by thymidine 3'-phosphorothioate and subsequent alkaline deblocking afforded the dinucleotide (Tps)2. The process of displacement and deblocking was repeated three more times at an average yield of 30 percent per step. The corresponding bifunctional derivative of deoxyadenosine was found much less reactive and practically unsuitable for repeated chain elongation. The ORD and CD spectra of the analogs are similar to those of the natural oligonucleotides.

Chromatography, DEAE-Cellulose↗
PubMed1988

Chemical structure of a new modified nucleoside located in the anticodon of Bombyx mori glycine tRNA2.

There are two species of glycine tRNA, tRNA(1Gly) and tRNA(2Gly), in the posterior silk glands of Bombyx mori. The first positions of their anticodons are guanosine and an unknown nucleoside for tRNA(1Gly) and tRNA(2Gly), respectively. This new nucleoside was isolated and the chemical structure was analyzed by thin layer chromatography and by UV, 1H-NMR, field desorption mass, and ORD spectroscopic measurements. The structure characterized by physical methods was finally confirmed by synthesis to be 5-((S)-carboxy(hydroxy) methyl)uridine methyl ester.

Animals↗
PubMed1989

Physicochemical properties of a human glycoprotein bearing blood group A activity.

A human erythrocyte glycoprotein was isolated and purified from blood of group A+1 by a procedure involving chloroform-methanol extraction and affinity chromatography on Helix pomatia lectin-Sepharose 6MB, and some of its physicochemical properties were determined. The resulting preparation was homogeneous as indicated by polyacrylamide gel electrophoresis. The glycoprotein contained nearly 60% carbohydrate and 40% protein. It was water-soluble and inhibited the agglutination of A-erythrocytes. Its molecular weight was 41,900 (amino acid analysis) or 55,200 (light scattering), whereas electrophoresis revealed two bands of 43,000 and 76,000 Da. The ORD spectrum was consistent with 30% alpha-helix, 20% beta-sheet, and 50% random coil. Intrinsic viscosity was 14.61 ml.g-1, partial specific volume was roughly 0.66, isoelectric and isoionic points were 6.90 and 6.95, respectively. The glycoprotein differs from glycophorin and appears to be one of the minor glycoproteins of the human erythrocyte membrane.

ABO Blood-Group System↗