Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “spatial structure”

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 1,639 records · Page 91Linked to original sources

[Experimental and theoretical conformation analysis of the O-antigenic polysaccharide from Pseudomonas cepacia strain 3181. I. Disaccharide links].

Nuclear Overhauser effects, with preirradiation of glycoside bond anomeric protons, coupling constants 3J C3, H1' and 3J C1', H4 and linkage optical rotations A were measured for L-Rha beta 1-3-L-Rha alpha 1-OMe and L-Rha alpha 1-3-L-Rha alpha 1-OMe which are the models of the disaccharide units of the Pseudomonas cepacia polysaccharide. Theoretical conformational analysis was carried out in terms of a mechanical molecular model approximation. The spatial structures of these disaccharides as well as of D-Rha alpha 1-2-D-Rha beta 1-OMe in aqueous solutions were discussed basing on the obtained results.

Antigens, Bacterial↗

[Experimental and theoretical conformation analysis of the O-antigenic polysaccharide from Pseudomonas cepacia strain 3181. II. The polysaccharide].

The spatial structure of Pseudomonas cepacia 3181 polysaccharide in aqueous solution is discussed basing on the data of nuclear Overhauser effect, observed with preirradiation of anomeric protons of all 3 D-rhamnose residues in the repeat unit, and theoretical conformational analysis. It is shown that conformational states of the free disaccharides and corresponding disaccharide units of the polysaccharide are similar. All conformations of the polysaccharide may be described by one shape representing an extended structure with characteristic turns in the D-Rha alpha 1-2-D-Rha beta 1-3-D-Rha units.

Antigens, Bacterial↗

[Determination of interproton distances in peptides by two-dimensional nuclear Overhauser effect spectroscopy (NOESY). Conformation of a cyclic analog of substance P in a solution].

Quantitative method is developed for evaluation interproton distances in peptides in solution. The method is based on the measurement of the relative intensities of the cross-peaks in the pure-phase absorption NOESY spectra. The ratios of the cross-peak intensities IN alpha/I alpha N and INN/I alpha N enable to determine the corresponding interproton distances dN alpha, d alpha N and dNN for several amino acid residues. These distances can be used to estimate other distances with cross-peaks in NOESY spectra. As example, the interproton distances are determined in a cyclic hexapeptide, namely cyclic analogue of substance P: cyclo [H-Glu-Phe-Phe-Gly-Leu-Met-NH(CH2)3-NH-]. The spatial structure of the molecule in dimethylsulphoxide solution is established.

Magnetic Resonance Spectroscopy↗

[Localization of antigenic determinants on a molecule of trophoblast-specific beta 1-glycoprotein].

Spatial localization of antigenic determinants of trophoblast-specific beta I-glycoprotein (TSG) has been elucidated using chemical modifications of the sugar and protein moieties of the molecule. Various deglycosylation procedures of TSG afforded fragments slightly soluble even in the presence of powerful detergents. Treatment of TSG with boric acid and its salts, accompanied with a conformational change of the sugar moiety, failed to alter conformation of the protein portion as evidenced by CD spectral data. This modification was found to increase the antigenic activity of TSG only scarcely. Modification of tryptophane or tyrosine residues of TSG changed spatial structure of the protein portion to can be a considerable loss of the TSG antigenic activity. The data obtained led to the conclusion that antigenic determinants of TSG are localized at the protein portion of the molecule and are topographic. A tryptophane residue is an indispensable constituent of the antigenic determinants.

Circular Dichroism↗

[The role of tryptophan residues in the antigenic activity of carcinoembryonic antigen].

Antigenic determinants of carcino-embryonic antigen (CEA) were spatially located using N-bromosuccinimide modification of tryptophan residues both in native (acetate buffer solution) and unfolded (guanidinium chloride solution) molecule of the antigen. Modification of exposed tryptophan residues failed to alter CEA antigenic activity and conformation of its protein portion as shown by CD spectroscopy. On the contrary, modification of buried tryptophan residues induced conformational changes of CEA protein portion connected with a considerable loss of its antigenic activity. It was shown that CEA antigenic activity depends on spatial structure of its protein moiety.

Bromosuccinimide↗

[Conformation properties and enzymatic activity of pancreatic ribonuclease in soluble complexes with sodium dextran sulfate].

Effect of complex formation with dextran sulfate (DS) (substitution degree 1.3, molecular mass 500 thousand) on RNAse enzymic activity. its spatial structure and conformation stability was studied. Hydrolytic activity of the enzyme in complex in inhibited already at small additions of DS, while the transferase one is changed only at a great excess of the polyelectrolyte. It has been shown by CD spectra that no notable conformation changes proceed in the enzyme during complex formation, although the enzyme turns destabilized to the denaturing effect of heat at the expense of strengthened interactions between DS and RNAse during its denaturation. Thus the inhibition of hydrolytic activity in the complex is primarily related to limitations for the formation of the enzyme-substrate complex on polyelectrolyte charged likely with the substrate, and not to the protein conformation changes.

Circular Dichroism↗

[Conformation-activity relations of des-Arg9-bradykinin. I. Conformation of molecules in solution].

The spatial structure of [des-Arg9]bradykinin, a selective agonist of the B1 type kinin receptors, was studied by means of theoretical conformational analysis. In order to restrict the number of conformations under consideration, we used available data on 1H NMR in (CD3)2SO solution indicating the C-terminal carboxyl group to interact with the guanidine group of Arg1 and the hydroxyl group of Ser6. The calculated set of [des-Arg9]bradykinin low-energy conformations was compared with the 1H NMR data. Four types of conformations were selected, which are consistent with experimental data and serve as sterically reliable models for the preferable three-dimensional structure of [des-Arg9]bradykinin in solution.

Amino Acid Sequence↗

Assessing the significance of the correlation between two spatial processes.

Modified tests of association based on the correlation coefficient or the covariance between two spatially autocorrelated processes are presented. These tests can be used both for lattice and nonlattice data. They are based on the evaluation of an effective sample size that takes into account the spatial structure. For positively autocorrelated processes, the effective sample size is reduced. A method for evaluating this reduction via an approximation of the variance of the correlation coefficient is developed. The performance of the tests is assessed by Monte Carlo simulations. The method is illustrated by examples from geographical epidemiology.

Adult↗

[Interrelation of conformational changes of crustacin and its capacity to bind specifically with carcino-embryonic antigen].

Temperature-, ionic strength-, calcium ion- and pH-dependence of spatial structure of crustacin have been studied using CD and fluorescent spectroscopy. Secondary structure of crustacin was estimated by CD spectra. An irreversible conformational transition of crustacin's protein moiety connected with the loss of CEA-binding activity has been found at ca. 50 degrees C. Crustacin is shown to be calcium-binding protein, stability of the native crustacin conformation being markedly enhanced by calcium ions (1 mM Ca2+ shifted up the transition temperature by approximately 10 degrees C). Calcium binding and ionic strength increase led to alteration of both secondary and tertiary structures of crustacin. The highest CEA-binding activity was observed for the calcium-bond form of crustacin. A lack of specific interaction of crustacin with some saccharides was shown. Interrelation between conformation and immunochemical activity of crustacin is discussed.

Calcium↗

The contribution of GABA-mediated inhibitory mechanisms to visual response properties of neurons in the kitten's striate cortex.

The effect of the microiontophoretic administration of the GABA antagonist bicuculline methiodide (BMI) on the responses of striate cortical neurons to light stimulation was investigated in kittens ranging in age between 11 and 28 d. The orientation sensitivity of the majority of the 88 neurons tested for this parameter decreased (40%) or was eliminated (18%) following the administration of BMI. Changes were seen in all layers and in all neuronal types, and the proportions of neurons that changed their orientation specificity were about the same during the second, third, and fourth postnatal weeks. Twenty-eight percent of the neurons were not affected in their orientation sensitivity by BMI. These neurons were recorded at all postnatal ages; they were located preferentially in layers IV and VI; and they had unimodal, bimodal, or ON-OFF mixed receptive fields. The remaining 14% of the neurons were initially unresponsive or responded in an erratic way to visual stimulation. These neurons became responsive and even exhibited orientation-specific responses during administration of BMI. The majority (56%) of direction-specific neurons became direction-nonspecific after the administration of BMI. Seventeen percent preserved some direction specificity, whereas 27% did not show any change at all. The effects of BMI on direction sensitivity were seen at all postnatal ages and on all neuronal types throughout layers III-VI. The majority of neurons unaffected by BMI in their direction sensitivity resided in layer VI. In those cases where orientation sensitivity was reduced, direction sensitivity (if present) was usually diminished as well. However, some neurons were found in which only 1 of the 2 parameters was significantly changed by BMI. The spatial structure of the receptive field, as revealed by stationary stimulation, was changed significantly by BMI in about half the neurons tested. A straightforward correlation between the alteration of orientation and/or direction sensitivity and changes in receptive-field structure was not found. The results demonstrate that, in the immature striate cortex, receptive-field properties of many neurons are determined by inhibitory processes mediated by GABA, which may also dictate the actual visual responsiveness of the neurons. The dissociations in the effects of BMI on orientation sensitivity, direction sensitivity, and receptive-field substructure indicate that the synaptic organization responsible for the various functional parameters is unlikely to be the same.

Animals↗

[Spatial organization of the N-terminal beta-endorphin tridecapeptide].

Using conformational analysis spatial structure and conformational properties of the N-terminal tridecapeptide--endorphine molecules were investigated. Calculations were based on the fragmental analysis using non-valent, electrostatic, torsional interactions and hydrogen bonds. It was shown that tridecapeptide could exist in several low-energetical conformational states. Enkephaline fragments structure depends on the most perspective structure of free metioninenkephaline. The results can be used for conformational analysis of endorphine molecules, for structure--function relations study.

Endorphins↗

Membrane skeleton alteration--a factor promoting IgG receptor expression in the erythrocyte membrane.

IgG receptor expression after selective cross-linking of spectrin by means of diamide was investigated. A diamide concentration dependent IgG loading of erythrocytes was observed. Furthermore, diamide causes disturbance of lipid asymmetry, decrease of the anisotropy after topooptical staining of the glycocalyx, increase of the phagocytosis index and aggregation of the IMP's. Our findings support the hypothesis that the arrangement of the membrane skeleton at the inner aspect of the membrane is decisive not only for the lipid asymmetry but also for the spatial structure of the glycocalyx at the outer aspect of the membrane and thus for the degree of exposure and arrangement of IgG-receptors, which are thought to be localized at an extracellular portion of band 3 protein.

Anion Exchange Protein 1, Erythrocyte↗

[Determination of the degree of collagen coiling by electron paramagnetic resonance].

It has been shown that kinetics of the death of free radicals UV-induced at 77 degrees K in collagen is determined by two reactions having different rates. Such shape of the kinetic curve is substantiated by the spatial structure of macromolecules and permits to find easily the portion of peptide chains in the helical form and the portion of end peptides not incorporated in this structure. The degree of helical pattern of collagen from rat skin was shown to be 92%.

Animals↗

[Synthesis and analysis of des-Met5-[D-Ala2]enkephalinamide analogs].

The effects of N- and C-terminal oligoalanine insertions into des-Met5-[D-Ala2]enkephalin amide (I) on the biological activity and spatial structure were examined. The corresponding analogues were obtained by solid-phase synthesis using Sephadex LH-20 ac a polymeric support. Biological activity was assayed via changes in the pain threshold in the rat, body temperature, and also as affinity for opiate receptors. Active analogues were obtained upon modifying the carboxylic group in the tetrapeptide I with di- and tri-D-alanyls. The CD spectra of the C-derivatized analogyes were similar to those of the starting tetrapeptide I and [Met5]enkephalin, whereas the N-derivatized analogues showed essentially different CD spectra.

Amino Acids↗

[1H-NMR study of the peptide corresponding to the ACTH-like sequence of the variable region of human G1 Eu heavy chain immunoglobin].

Synthetic decapeptide corresponding to ACTH-like sequence of the variable part of the heavy chain of immunoglobulin G1 Eu was studied by two-dimensional 1H-NMR spectroscopy (400 MHz). A complete assignment of signals in the peptide spectrum was made. The decapeptide was shown not to have any ordered spatial structure, and was characterized by a high extent of flexibility of the oligopeptide chain, except for the peptide bond with an N-terminal residue.

Adrenocorticotropic Hormone↗

[Principles of quantitative analysis of two-dimensional spectra of nuclear Overhauser effect in evaluation of protein and peptide conformation].

To elucidate potentialities of two-dimensional homonuclear Overhauser effect (NOESY) spectra of peptides and proteins for their spatial structure determination, impact of experimental parameters and intrinsic properties of the investigated molecule on proton cross-peak volumes in NOESY spectra was analysed. Recommendations which could increase accuracy of cross-peak volume measurements were suggested. Influence of intrinsic properties of a molecule (spin-lattice relaxation times T1, correlation time tau C and surrounding protons) on the volume of cross-peak for particular protons was analyzed using a complete relaxation matrix of the (formula; see text) helix of gramicidin A. Nonselective relaxation time T1 of the protons was found to affect only slightly the results of cross-peak volumes computer simulation, whereas correlation time tau C and surrounding protons seriously influenced cross-peak volumes. Nevertheless, cross-peak volumes between NH, C alpha H and C beta H protons of a dipeptide fragment of the entire molecule could be accurately simulated using the relaxation matrix of the individual dipeptide. Thus local conformations (torsion angles phi, psi and chi 1) of amino acid residues could be deduced independently of one another and prior to the complete analysis of a molecular structure. The result can be obtained even in the presence of spin-diffusion at mixing times providing maximal volumes of cross-peaks in NOESY spectra.

Magnetic Resonance Spectroscopy↗

[Effect of polymer modification of insulin on its enzymatic hydrolysis and conformation properties].

AI, B29 insulin polymeric derivatives in which the polymeric chains (N-polyvinylimidazole, N-polyvinylpyrrolydone and polyacrylic acid) are bonded to the insulin molecule at one point were synthesized. The hydrolysis of the modified insulin by trypsin is dependent to a great extent on the chemical nature of the modifying polymer and is virtually independent of its molecular weight up to 20 kD. The effect of the modifying polymer manifests itself mainly in a change of the Michaelis constant. Investigation of the conformational properties of the insulin derivatives by the method of optical rotatory dispersion revealed that insulin modification by polymers caused a decrease of the amino acid content in the alpha-helical sequence from 41 to 33-30%. The chemical nature of the modifying polymer and its molecular weight have a profound effect on the conformational stability of the residual spatial structure of the modified insulin in alkaline media.

Amino Acids↗

Expression of cDNAs encoding the precursor and the mature form of chicken mitochondrial aspartate aminotransferase in Escherichia coli.

Both the precursor and the mature form of chicken mitochondrial aspartate aminotransferase were synthesized in Escherichia coli. The precursor was found to sediment quantitatively together with insoluble cell material. In contrast, mature mitochondrial aspartate aminotransferase could be readily extracted from the cells and was indistinguishable from the enzyme isolated from chicken heart in all respects tested: specific activity 230 units mg-1; Mr 2 X 45,000; pI greater than 9; NH2-terminal sequence SSWWSHVEMG, the initiator methionine having been removed by the bacteria. Thus, the polypeptide chain representing mature mitochondrial aspartate aminotransferase is an autonomous folding unit which attains its functional spatial structure independently of the presence of the prepiece, trans-membrane passage, and proteolytic processing.

Amino Acid Sequence↗