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Results for “Structural changes”

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PubMed2001

Structural changes in bacteriorhodopsin during the photocycle measured by time-resolved polarized Fourier transform infrared spectroscopy.

The structural changes in bacteriorhodopsin during the photocycle are investigated. Time resolved polarized infrared spectroscopy in combination with photoselection is used to determine the orientation and motion of certain structural units of the molecule: Asp-85, Asp-96, Asp-115, the Schiff base, and several amide I vibrations. The results are compared with recently published x-ray diffraction data with atomic resolution about conformational motions during the photocycle. The orientation of the measured vibrations are also calculated from the structure data, and based on the comparison of the values from the two techniques new information is obtained: several amide I bands in the infrared spectrum are assigned, and we can also identify the position of the proton in the protonated Asp residues.

Aspartic Acid↗

PubMed2005

Age-related structural changes in the young adult brain shown by magnetic resonance diffusion tensor imaging.

RATIONALE AND OBJECTIVE: Structure of the brain is generally thought to remain stationary over the course of young adulthood. However, there is some evidence that microstructural changes of the brain do occur during this period. Magnetic resonance diffusion tensor imaging (DTI) provides quantitative measures of structural changes in the brain. We used DTI to detect possible age-related structural changes in the brains of young adults. MATERIALS AND METHODS: Twenty-five healthy adults in their 20s and 30s were studied using DTI. Maps of mean diffusivity and fractional anisotropy (FA) were created for subsequent histogram and region-of-interest analyses, and the results were correlated with the respective ages of the subjects. RESULTS: The histogram analysis revealed a significant increase in the mean FA value (r = 0.407, P < .05) and a significant decrease in FA peak height (r = -0.578, P < .002) with increasing age. No age-related changes were observed in indices derived from mean diffusivity maps. Region-of-interest analysis showed no focal white matter regions with significant FA change. CONCLUSION: Quantitative DTI revealed age-related structural changes in the brains of young adults. Changes on FA histograms observed in this study were considered to be related to changes in the relative volumes of gray and white matter and may represent maturational changes.

Adult↗

PubMed2004

Effect of sulfated polysaccharides on heat-induced structural changes in beta-lactoglobulin.

The mechanism that leads to a decreased aggregation of beta-lactoglobulin in the presence of dextran sulfate and lambda-carrageenan was investigated by assessing changes in the denaturation thermodynamics and protein structure. Differential scanning calorimetry results showed that the denaturation temperature (Tp) was about 4.6 degrees C higher in the presence of dextran sulfate, as compared with beta-lactoglobulin alone, whereas in the presence of lambda-carrageenan the difference in Tp was about 1.2 degrees C. Changes in protein structure studies using near-UV circular dichroism (CD) provided support for the calorimetric results. The transition midpoint (Tm) for denaturation of beta-lactoglobulin was about 5 degrees C higher in the presence of dextran sulfate than that found with beta-lactoglobulin alone and about 2 degrees C in the presence of lambda-carrageenan. Thermal modifications of the tertiary structure of beta-lactoglobulin were irreversible at temperatures above 67 degrees C; the addition of dextran sulfate reduced the extent of such modifications. Far-UV CD studies indicated that the addition of dextran sulfate or lambda-carrageenan did not affect secondary structure changes of beta-lactoglobulin upon heating. These studies indicate that dextran sulfate and lambda-carrageenan can enhance the stability of beta-lactoglobulin and thereby inhibit heat denaturation and aggregation.

Carrageenan↗

PubMed2006

Relation between radiation-induced whole lung functional loss and regional structural changes in partial irradiated rat lung.

PURPOSE: Radiation-induced pulmonary toxicity is characterized by dose, region, and time-dependent severe changes in lung morphology and function. This study sought to determine the relation between the structural and functional changes in the irradiated rat lung at three different phases after irradiation. MATERIALS AND METHODS: Six groups of animals were irradiated to 16-22 Gy to six different lung regions, each containing 50% of the total lung volume. Before and every 2 weeks after irradiation, the breathing rate (BR) was measured, and at Weeks 8, 26, and 38 CT was performed. From the computed tomography scans, the irradiated lung tissue was delineated using a computerized algorithm. A single quantitative measure for structural change was derived from changes of the mean and standard deviation of the density within the delineated lung. Subsequently, this was correlated with the BR in the corresponding phase. RESULTS: In the mediastinal and apex region, the BR and computed tomography density changes did not correlate in any phase. After lateral irradiation, the density changes always correlated with the BR; however, in all other regions, the density changes only correlated significantly (r(2) = 0.46-0.85, p < 0.05) with the BR in Week 26. CONCLUSION: Changes in pulmonary function correlated with the structural changes in the absence of confounding heart irradiation.

Animals↗

PubMed1995

Solution structure of (Cd2+)1-calbindin D9k reveals details of the stepwise structural changes along the Apo-->(Ca2+)II1-->(Ca2+)I,II2 binding pathway.

The three-dimensional solution structure of (Cd2+)1-calbindin D9k has been determined by distance geometry, restrained molecular dynamics and relaxation matrix calculations using experimental constraints obtained from two-dimensional 1H and 15N-1H NMR spectroscopy. The final input data consisted of 1055 NOE distance constraints and 71 dihedral angle constraints, corresponding to 15 constraints per residue on average. The resulting ensemble of 24 structures has no distance or dihedral angle constraints consistently violated by more than 0.07 A and 1.8 degrees, respectively. The structure is characteristic of an EF-hand protein, with two helix-loop-helix calcium binding motifs joined by a flexible linker, and a short anti-parallel beta-type interaction between the two ion-binding sites. The four helices are well defined with a root mean square deviation from the mean coordinates of 0.35 A for the backbone atoms. The structure of the half-saturated cadmium state was compared with the previously determined solution structures of the apo and fully calcium saturated calbindin D9k. The comparisons were aided by introducing the ensemble averaged distance difference matrix as a tool for analyzing differences between two ensembles of structures. Detailed analyses of differences between the three states in backbone and side-chain dihedral angles, hydrogen bonds, interatomic distances, and packing of the hydrophobic core reveal the reorganization of the protein that occurs upon ion binding. Overall, it was found that (Cd2+)1-calbindin D9k, representing the half-saturated calcium state with an ion in site II, is structurally more similar to the fully calcium-saturated state than the apo state. Thus, for the binding sequence apo-->(Ca2+)II1-->(Ca2+)I,II2, the structural changes occurring upon ion binding are most pronounced for the first binding step, an observation that bears significantly on the molecular basis for cooperative calcium binding in calbindin D9k.

Animals↗

PubMed1976

Novel mutation that causes a structural change in a lipoprotein in the outer membrane of Escherichia coli.

A novel mutation which caused a structural change in a lipoprotein in the outer-membrane has been found in Escherichia coli K-12. The lipoprotein of the wild-type strain is known to have a peculiar amino terminal structure: glycerylcysteine with two fatty acids attached by ester linkages and one fatty acid by an amide linkage. In contrast to the wild-type lipoprotein, the mutant lipoproteins is isolated from the E. coli envelope as a dimer of molecular weight of about 15,000. The dimer can be reduced by mercaptoethanol to the lipoprotein monomer of molecular weight of about 7,500. The monomer has a free thiol group which is susceptible to monoiodacetie mutant lipoprotein is extremely low in comparison with that into the wild-type lipoprotein. These results suggest that the mutant is defective in transferring a glycerol group to the thiol group of the amino terminal cysteine residue of the lipoprotein. The gene responsible for this modification reaction has been located at 36.5 min on the E. coli chromosome.

Bacterial Proteins↗

PubMed1996

Structural changes in the peptide backbone in complex formation between activated rhodopsin and transducin studied by FTIR spectroscopy.

Structural changes in the complex formation between transducin and metarhodopsin II, the activated form of photolyzed rhodopsin, in visual transduction processes were analyzed by Fourier transform infrared spectroscopy. The spectrum of the complex was obtained by subtracting the contribution of metarhodopsin I and uncomplexed metarhodopsin II. The averaged spectrum upon the complex formation was then compared with that in the conversion of rhodopsin-to-metarhodopsin II. Frequency shifts of the peptide carbonyl vibrations at 1686, 1674, and 1661 cm-1 to 1640 cm-1 were observed upon complex formation from metarhodopsin II plus transducin. These changes must have resulted from the strengthening of H-bonding of one or a few peptide groups but is not ascribable to global conformation change. Changes in the frequencies of the peptide amides were also detected. With regard to intramembrane carboxylic acid residues, no further changes were noticed in the carboxyl vibrations of Asp83, Glu122, and Glu113. Only a small change possibly due to Glu134 was detected.

Animals↗

PubMed1988

Lithium-induced structural changes in the cortical distal nephron localized by computer-assisted three-dimensional reconstruction.

Lithium treatment is known to cause tubule dilation in distal nephron segments both in rat and in man. However, due to the heterogeneous cell composition of the distal nephron and the cellular changes following lithium treatment, it has been difficult to identify the structurally changed segments. In this study we have therefore applied computer-assisted reconstruction of cortical distal nephron segments. Tubule dilation was demonstrated in connecting and initial collecting tubules and in the first part of cortical collecting ducts (CCD) whereas it was absent from distal straight and distal convoluted tubules. Principal cells (P cells) in the CCD showed swelling of the cytoplasm, accumulation of actin-like microfilaments, and abnormal arrangements of basolateral membranes. Connecting tubule cells (CNT cells) showed similar but less pronounced changes. Intercalated cells (I cells) showed an accumulation of vesicles in the apical cytoplasm and a reduced luminal surface area. Lesions in P and CNT cells may, at least in part, explain the diabetes insipidus and sodium loss found during lithium treatment. Proton secretion in I cells is probably mediated by an ATPase present in the luminal membrane. The reduction in area of this membrane may explain why lithium-treated animals have a lowered ability to excrete an acid load.

Animals↗

PubMed1995

Photoinduced structural changes in the collagen/gelatin binding domain of fibronectin.

Prolonged exposure of human plasma fibronectin (pFn) and its 40- and 21-kDa collagen/gelatin binding fragments (GBFs) to 280-nm irradiation decreased their affinity for gelatin and for TR-CB7, a fluorescently labeled CNBr fragment of the alpha-1 chain of type I collagen. Fluorescence polarization binding assays of TR-CB7 with pFn and the 40-kDa GBF yielded progressively higher Kd's with increased time of exposure to 280-nm light at 25 degrees C. Binding of nonirradiated and irradiated pFn and fragments to gelatin-Sepharose correlated with the polarization data, confirming diminished gelatin binding following exposure to 280-nm light. Fluorescence spectra of intrinsic tryptophans in the 21- and 40-kDa GBFs exhibited changes indicative of photoinduced conformational changes; the maximum fluorescence wavelength red-shifted from between 340 and 350 nm to 360 nm, with concomitant increases in fluorescence intensity. Exposure of 21- and 40-kDa GBFs and pFn to 280-nm light also generated approximately two, four, and six free sulfhydryl groups per molecule, respectively. No sulfhydryl release was observed in other Trp- and disulfide-containing proteins under the same conditions. We propose that the fluorescence changes as well as the changes in affinity for gelatin or the collagen fragment result from structural changes secondary to the breakage of disulfide bonds, as a consequence of energy transfer from nearby tryptophans in one or more of the Fn type I repeats in the gelatin binding region of fibronectin.

Collagen↗

PubMed2006

Experimental versus expected halide-ion size differences; structural changes in three series of isotypic bismuth chalcogenide halides.

Experimentally determined halide-ion size differences are compared with expected size differences in the three series of isotypic bismuth chalcogenide halide compounds, KBi(6)O(9)X (X = Cl, Br and I), BiOX (X = F, Cl, Br and I) and BiSX (X = Cl, Br and I). The strong deviations observed can be assigned to steric strain caused by the heterogeneity of the bond-valence pattern and (for BiOX) to anion-anion repulsion and a change in the connectivity scheme. Some special features of the BiOF structure and the question of "isotypism" within the BiOX series are briefly discussed. Structural changes within the BiSX series are analysed.

Journal Article↗

PubMed2005

Association between age and knee structural change: a cross sectional MRI based study.

OBJECTIVE: To describe the associations between age, knee cartilage morphology, and bone size in adults. METHODS: A cross sectional convenience sample of 372 male and female subjects (mean age 45 years, range 26-61) was studied. Knee measures included a cartilage defect five site score (0-4 respectively) and prevalence (defect score of > or =2 at any site), cartilage volume and thickness, and bone surface area and/or volume. These were determined at the patellar, medial, and lateral tibial and femoral sites using T(1)weighted fat saturation MRI. Height, weight, and radiographic osteoarthritis (ROA) were measured by standard protocols. RESULTS: In multivariate analysis, age was significantly associated with knee cartilage defect scores (beta = +0.016 to +0.073/year, all p<0.01) and prevalence (OR = 1.05-1.10/year, all p<0.05) in all compartments. Additionally, age was negatively associated with knee cartilage thickness at all sites (beta = -0.013 to -0.035 mm/year, all p<0.05), and with patellar (beta = -11.5 microl/year, p<0.01) but not tibial cartilage volume. Lastly, age was significantly positively associated with medial and lateral tibial surface bone area (beta = +3.0 to +4.7 mm(2)/year, all p<0.05) and patellar bone volume (beta = +34.4 microl/year, p<0.05). Associations between age and tibiofemoral cartilage defect score, cartilage thickness, and bone size decreased in magnitude after adjustment for ROA, suggesting these changes are directly relevant to OA. CONCLUSION: The most consistent knee structural changes with increasing age are increase in cartilage defect severity and prevalence, cartilage thinning, and increase in bone size with inconsistent change in cartilage volume. Longitudinal studies are needed to determine which of these changes are primary and confirm their relevance to knee OA.

Adult↗

PubMed2006

Structural changes of cross-bridges on transition from isometric to shortening state in frog skeletal muscle.

Structural changes in the myosin cross-bridges were studied by small-angle x-ray diffraction at a time resolution of 0.53 ms. A frog sartorius muscle, which was electrically stimulated to induce isometric contraction, was released by approximately 1% in 1 ms, and then its length was decreased to allow steady shortening with tension of approximately 30% of the isometric level. Intensity of all reflections reached a constant level in 5-8 ms. Intensity of the 7.2-nm meridional reflection and the (1,0) sampling spot of the 14.5-nm layer line increased after the initial release but returned to the isometric level during steady shortening. The 21.5-nm meridional reflection showed fast and slow components of intensity increase. The intensity of the 10.3-nm layer line, which arises from myosin heads attached to actin, decreased to a steady level in 2 ms, whereas other reflections took longer, 5-20 ms. The results show that myosin heads adapt quickly to an altered level of tension, and that there is a distinct structural state just after a quick release.

Actins↗

PubMed2004

Evaluation of structural changes induced by high hydrostatic pressure in Leuconostoc mesenteroides.

Scanning electron microcopy (SEM), transmission electron microscopy (TEM), and differential scanning calorimetry (DSC) were used to evaluate structural changes in Leuconostoc mesenteroides cells as a function of high-hydrostatic-pressure treatment. This bacterium usually grows in chains of cells, which were increasingly dechained at elevated pressures. High-pressure treatments at 250 and 500 MPa also caused changes in the external surface and internal structure of cells. Dechaining and blister formation on the surface of cells increased with pressure, as observed in SEM micrographs. TEM studies showed that cytoplasmic components of the cells were affected by high-pressure treatment. DSC studies of whole cells showed increasing denaturation of ribosomes with pressure, in keeping with dense compacted regions in the cytoplasm of pressure-treated cells observed in TEM micrographs. Apparent reduction of intact ribosomes observed in DSC thermograms was related to the reduction in number of viable cells. The results indicate that inactivation of L. mesenteroides cells is mainly due to ribosomal denaturation observed as a reduction of the corresponding peak in DSC thermograms and condensed interior regions of cytoplasm in TEM micrographs.

Calorimetry, Differential Scanning↗

PubMed2004

[Dynamics of structural changes of Paramecium caudatum and Bursaria truncatella macronuclear chromatin and nucleoli under hypotonic conditions].

Dynamics of structural changes of nucleoli, complex nucleolar aggregates and chromatin bodies in macronuclei (Ma) of ciliates Paramecium candatum and Bursaria truncatella under hypotonic conditions was studied. It was shown that after a 3 min hypotonic treatment nuclei swelled and became highly vacuolated. 3D-reconstruction showed that such nucleoli were formed by nucleolonema-like threads about 100-200 nm in thickness. Intranucleolar chromatin bodies decompacted, but remained bound with fibrillar component of the nucleolus by thin fibres about 10 nm thick. After 6 min hypotonic treatment the nucleolar material loosened and had a "gauze", or network-like appearence. After 10 min hypotonic treatment nucleoli dissociated completely. It was shown that a transition of chromatin bodies from completely compact to partially and fully decompacted state occurred cooperatively in different regions of Ma. In particular, chromatin bodies in the central part of complex nucleolar aggregates decompacted much faster than those in the Ma karyoplasm. It evidences for a specific, well-ordered chromatin organization in Ma. Prolonged hypotonic treatment led to a complete dissociation of Ma components; fibres 6-10 nm thick were solely observed in such preparations. Such fibres may represent remnant structures of the nuclear matrix. Dynamics of Ma chromatin bodies decompaction correlates well with that of chromomeres in the nuclei of higher eukaryotes. Our data confirm that chromatin 100-200 nm bodies in the ciliate Ma are analogues of chromomeres--looped discrete chromatin domains, observed in the nuclei of higher eukaryotes.

Animals↗

PubMed2001

[Mechanical properties of weld area soldered by lasers and structural changes in hot reaction zone].

OBJECTIVE: To analyse and measure the welding depths and strengths of three kinds of welding materials under different laser welding conditions as well as the structural changes of the heat affected zone. METHODS: Under different voltages and pulse duration three kinds of measuring sticks, including Co-Cr alloy, Ni-Cr alloy and pure titanium were welded and their strengths were compared with that of control group. At the same time, the structure of the heat-affected zone was analysed by means of the gold-phase method. RESULTS: The welding depth and strength of Co-Cr alloy were in direct proportion to the setting voltage, with averages of 335MPa (250V) to 573MPa(330V). At the heat-affected zone, the crystal particle was small and the end point of welding by laser bean presented the shape of the mountain peak and the interval of finger shape. The center of measuring sticks had a black zone with the circle shape. The setting voltage was in direct proportion to the welding depth of pure titanium and in inverse proportion to the welding strength with averages of 221MPa(250V) to 154MPa (330V). The crystal particle in the heat affected zone grew large and the solid phase expanded, the interval of the crystal oxidised, and the structure showed honeycomb changes. CONCLUSION: The laser welding is favourable to the welding properties of Co-Cr and Ni-Cr alloys, but its effect on the welding properties of pure titanium needs further discussion.

Biomechanical Phenomena↗

PubMed2001

pH dependent conformational and structural changes of xylanase from an alkalophilic thermophilic Bacillus sp (NCIM 59).

The pH induced conformational and structural changes of Xyl II have been investigated from the alkalophilic thermophilic Bacillus sp. using kinetic, circular dichroism and fluorescence spectroscopy studies. The systematic studies on the folding and stability of cellulase-free xylanases are important, since their biotechnological applications require them to function under extremes of pH and temperature. The Trp fluorescence and the kinetic constants were found dependent on the pH. Above pH 8, the enzyme exhibited unfolding transitions as revealed by a red shift in the emission maximum as well as decreases in the fluorescence intensity. Circular dichroism studies revealed a decrease in the CD ellipticity at 222 nm at pH 9 and 10. The reduced catalytic activity of Xyl II at alkaline pH is correlated to the pH induced unfolding and ionization or protonation of key protein residues. The pH profile of Xyl II showed apparent pK values of 5.5 and 7 for the free enzyme and 5.6 and 6.7 for the enzyme-substrate complex. The abnormally high pK of 6.7 indicated the participation of a carboxyl group present in a non-polar environment. The pH dependence of inactivation kinetics of Xyl II with Woodward's reagent K corroborates evidence for the presence of a catalytically important carboxyl residue. The sequence alignment studies of Xyl II, in combination with kinetic and chemical modification data provide strong evidence for the participation of Asp94 in the catalytic function. The Xyl II produced from an alkalophilic source, was stable at pH 10 with a t(1/2) of 24 h. However, the enzyme exhibited pH optimum at near neutral values, which can be explained by the ionization and microenvironment of the active site residues.

Journal Article↗

PubMed1987

Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.

Electron microscopy has been used to study the structural changes that occur in the myosin filaments of tarantula striated muscle when they are phosphorylated. Myosin filaments in muscle homogenates maintained in relaxing conditions (ATP, EGTA) are found to have nonphosphorylated regulatory light chains as shown by urea/glycerol gel electrophoresis and [32P]phosphate autoradiography. Negative staining reveals an ordered, helical arrangement of crossbridges in these filaments, in which the heads from axially neighboring myosin molecules appear to interact with each other. When the free Ca2+ concentration in a homogenate is raised to 10(-4) M, or when a Ca2+-insensitive myosin light chain kinase is added at low Ca2+ (10(-8) M), the regulatory light chains of myosin become rapidly phosphorylated. Phosphorylation is accompanied by potentiation of the actin activation of the myosin Mg-ATPase activity and by loss of order of the helical crossbridge arrangement characteristic of the relaxed filament. We suggest that in the relaxed state, when the regulatory light chains are not phosphorylated, the myosin heads are held down on the filament backbone by head-head interactions or by interactions of the heads with the filament backbone. Phosphorylation of the light chains may alter these interactions so that the crossbridges become more loosely associated with the filament backbone giving rise to the observed changes and facilitating crossbridge interaction with actin.

Actin Cytoskeleton↗

PubMed1989

Left ventricular structural changes in young men at increased risk of developing essential hypertension. Assessment by echocardiography.

Left ventricular structural changes were assessed by echocardiography in young men at increased risk of developing essential hypertension. Four groups were investigated: 28 normotensive offspring of hypertensives (NTO), 20 borderline hypertensive offspring of hypertensives (BHO), 12 borderline hypertensives with normotensive parents (BH) and 28 normotensive subjects with normotensive parents (NT). The septum-posterior wall ratio was increased in the risk groups (NT, BHO, BH). The increased ratio could be explained by both heredity and elevated blood pressure. Left ventricular mass index (LVMI) correlated strongly with physical activity in the NT group, so LVMI was adjusted accordingly. The adjusted LVMI was significantly increased in the risk groups. The increase in the adjusted LVMI could best be explained by the elevated blood pressure and not by heredity. Multivariate analysis of variance showed that physical activity is an independent predictor of LVMI only in the NT group and that systolic blood pressure is an independent predictor of LVMI only in the risk groups.

Adolescent↗