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PubMed1998

Anesthetic-induced structural changes in the nicotinic acetylcholine receptor.

The difference between infrared spectra of the nicotinic acetylcholine receptor (nAChR) recorded in the absence and presence of the agonist carbamylcholine (Carb) reveals a complex pattern of positive and negative bands that provides a spectral map of Carb-induced structural change. This spectral map is affected by the presence of either the local anesthetic, dibucaine, or the short chain alcohol, propanol. Both antagonists alter the intensities of difference bands in a manner consistent with the stabilization of a desensitized state. Spectral variations are also observed that are indicative of both the displacement of the anesthetics from the nAChR upon the addition of Carb and physical interactions that occur between the anesthetics and binding site residues.

Anesthetics↗

PubMed1994

pH-induced structural changes in human serum apotransferrin. pKa values of histidine residues and N-terminal amino group determined by 1H-NMR spectroscopy.

The binding of apotransferrin (80 kDa) to the transferrin receptor is known to be highly pH-dependent. We have investigated pH-induced structural changes in human serum apotransferrin over the pH* (meter reading in D2O solutions) range 2.5-11 using 1H-NMR spectroscopy. The pKa values of 14 (possibly 15) of the 19 His residues in the protein have been determined as well as that of the terminal amino group (Val1, 7.75). About eight His residues deprotonate when the pH* is raised from the endosomal value of about 5.5 to the blood plasma value (7.4). Four His residues have pKa < 6. Sharp discontinuities in the His titration curves were observed below pH 4.3 and at pH 3.5 molten globule states were detected.

Apoproteins↗

PubMed1985

Nuclear protein, matrix and structural changes in rooster liver after estrogenic induction of vitellogenesis.

The estrogenic induction of vitellogenesis in avian and amphibian liver has been well characterized at the target gene level. Comparatively little however, is known about cognate nuclear events associated with the response, particularly those involving large-scale structural changes and the non-histone proteins (NHP). We have examined these aspects further in primary stimulated roosters. In the first 24 hr post induction with estradiol, hepatocyte nuclei enlarged by 50% and exhibited sharp rises in total protein and RNA content. In particular, the mass of residual NHP rose about 40%. Extensive internal reorganization was evident, including partial disaggregation of chromatin, proliferation of interchromatin components and de novo appearance of prominent "nuclear bodies". These changes were accompanied by quantitative fluctuations in nucleoplasmic and several matrix fraction proteins. A marked relative decrease was evident in all three lamins, as well as approximately 75 and approximately 175 kD proteins. Hn-RNP-associated polypeptides however, and various unidentified components became much more prominent. By 24 hr, cells were fully differentiated for bulk export of vitellogenin and low density lipoproteins. All changes persisted for several days before gradually regressing to normal over a 2-4 week period. Many key nuclear modifications, however, did not regress fully, including persistent enlargement, elevated NHP content and modified matrix fraction proteins. Collectively, these may reflect part of the "memory" effect, commonly observed in steroid target tissues, whereby a second, more pronounced response can be triggered long after primary induction has subsided.

Animals↗

PubMed1994

Structural changes of active site cleft and different saccharide binding modes in human lysozyme co-crystallized with hexa-N-acetyl-chitohexaose at pH 4.0.

Human lysozyme was co-crystallized with hexa-N-acetyl-chitohexaose, (GlcNAc)6, at pH 4.0 and 4.0 degrees C in a new orthorhombic form, where two protein molecules, MOL1 and MOL2, were contained in an asymmetric unit. The three-dimensional structure was refined to an R-factor of 17.0% at 1.6 A resolution. It was found that (GlcNAc)6 had already been cleaved to (GlcNAc)4 and (GlcNAc)2. In MOL1, (GlcNAc)4 was bound to the A, B, C, and D subsites, and binding sites of (GlcNAc)2 were close to the E and F subsites proposed on the basis of model building by Phillips and his colleagues. In MOL2, only the (GlcNAc)4 moiety could be found in the A, B, C and D subsites. Significant shifts of the backbone atoms were observed in the region of residues 102 to 120, which composed one side of the wall of the active site cleft. Consequently, the active cleft, with respect to the saccharide binding sites A, B and C, is narrower in both protein molecules. The residues 109 to 111 in site D of MOL1 are moved toward saccharide residue D, whereas those of MOL2 are only slightly shifted. In spite of these facts, the saccharide residues in site MOL1 and MOL2 are moved inside of the cleft. The distribution of water molecules and the hydrogen bond network in site D differ between the structures of MOL1 and MOL2. These structural changes in the active site cleft may be responsible for accommodating the substrate and releasing the products of hydrolysis. These results suggest that the three-dimensional structures of MOL1 and MOL2 remain in intermediate states between a transition state and an enzyme/product complex state.

Binding Sites↗

PubMed2006

Structural changes in poly(ethyleneimine) modified microemulsion.

The influence of branched poly(ethyleneimine) on the phase behavior of the system sodium dodecylsulfate/toluene-pentanol (1:1)/water has been studied. The isotropic microemulsions still exist when water is replaced with aqueous solutions of PEI (up to 30% in weight), but their stability is significantly influenced. From a polymer concentration of 20 wt%, the polymer enhances the solubilization of water in oil, changes the sign of the spontaneous curvature of the surfactant film, and induces an inversion of the microemulsion type from water-in-oil (L(2)) to oil-in-water (L(1)), by the formation of a bicontinuous channel. Further investigations show that the addition of polymer in the L(2) phase changes the droplet-droplet interactions as the conductivity drops and the percolation disappears. In the bicontinuous channel, higher viscosities can be detected, as well as a weak percolation followed by a steep increase of the conductivity, which can be related to evident structural changes in the system. DSC measurements allow then to follow the changes of the water properties in the system, from interfacial-water in the L(2) phase to free-water in the sponge-like phase. Finally, all the measurements performed permit to characterize the structural transitions in the system and to understand the role of the added polymer.

Calorimetry, Differential Scanning↗

PubMed1993

Structural changes of the interphotoreceptor matrix in an inherited retinal degeneration: a lectin cytochemical study of progressive rod-cone degeneration.

PURPOSE: In the retinal disorder progressive rod-cone degeneration (prcd) in miniature poodle dogs, the photoreceptor layer degenerates slowly in the course of 5 to 7 years. Components of the interphotoreceptor matrix form a continuous extracellular lattice around photoreceptors. The purpose was to study the photoreceptor cell-matrix interactions during the disease and degeneration phases. Because degeneration rate was slower in cones, the authors also wanted to investigate whether there was a link between the degeneration and the photoreceptor-specific interphotoreceptor matrix domains. METHODS: Rod- and cone-specific interphotoreceptor matrix domains were examined during two periods: before morphological signs of disease had appeared and during the degenerative stages. Two lectin probes were used; wheat germ agglutinin and peanut agglutinin. By their affinity for terminal carbohydrates, the lectins visually separated the two photoreceptor-specific domains and allowed follow-up of the fate of the rod and cone matrices separately. RESULTS: Before and during the course of disease, the lectin distribution in rod and cone domains remained normal, however, in the degenerative phase of the disease, there were structural changes in the matrix domains. The matrix connections between the individual domains was disrupted and single domains were formed. Cone domains and, to a lesser degree rod domains, were thickened around the inner and outer segments. CONCLUSIONS: The changes occurring in the photoreceptor-specific domains were indicative of structural adaptation to cell death and to degenerative conditions. There was no evidence of an active involvement of the interphotoreceptor matrix components studied in the disease process.

Animals↗

PubMedDate not supplied

[Structural changes in lipid membranes and collagen irradiated with UV light and the protective effect of plant extracts].

The results of experimental studies on the effect of UV irradiation on collagen, artificial lipid membranes, and rat skin, as well as the protective effect of plant extracts from UV radiation are presented. The irradiation of collagen and lipid membranes with solar and artificial UV light leads to structural changes in these objects. In particular, collagen molecules denature and transfer into a new conformational state. The effect of UV light on lipid membranes and liposomes leads to a disturbance of membrane structure, which is connected with a decrease in the number of lipid molecules involved in the cooperative transition from gel into a liquid crystal state. The components of plant extracts (mainly flavonoids) absorb UV radiation in the erythem-forming spectral area and block the destructive processes occurring in collagen and lipids.

Animals↗

PubMed1975

The regreening of nitrogen-deficient Chlorella fusca II. Structural changes during synchronous regreening.

Chlorella fusca, strain 211-15, cells degreened in a nitrogen-deficient mineral growth medium in the light for 4-6 weeks were regreened for up to 24 hrs in a nitrogen rich medium that leads to synchronous cell division at 24-26 hrs. Structural changes in the plastid membranes during the regreening period were observed by thin section and freeze-fracture electron microscopy. Nitrogen-deficient plastids were found to have non-appressed lamellae, prolamellar body-like membrane aggregations, and only 2 types of freeze-fracture face. At this time no photosynthetic oxygen evolution could be demonstrated. After 6 hrs regreening the plastid lamellae had fused to form bands of appressed lamellae and the four types of freeze-fracture face, described previously, were visible. At this time photosynthetic oxygen evolution could be demonstrated. After 24 hrs regreening the plastids had an appearance typical of normally grown Chlorella and had commenced to divide. Supporting evidence for these developmental stages is presented from isolated chloroplast particle fractions. An unusual type of cell wall proliferation was observed in the nitrogen-deficient Chlorella cells that resulted in the laying down of several walls, each with a trilaminar component.

Cell Division↗

PubMed1995

[Effect of structural changes in animal husbandry on the environment due to wastes and residues from animal production].

From the statistic data it can be taken, that especially in the old federal states of Germany, in the new future animal husbandry will be more and more concentrated in certain regions. This structural change probably is followed by a similar concentration process concerning slaughterhouses and within limitations the rendering industry too. This will result in a higher regional environmental pollution by volatile and soluble components as well as microorganism from agricultural wastes of animal origin, by offal and by products from slaughtering as well as by highly contaminated slaughterhouse wastewater and by pollutants in air and waste-water from rendering plants. Further regional environmental and epidemiological risks are connected with recycling of voluminous slaughterhouse wastes like rumen-, stomach- and gut-contents to the farms as fertilizers, unless strictly hygienic guidelines have to be followed in the future.

Abattoirs↗

PubMed1999

Reduced pH causes structural changes in the potent mitogenic toxin of Pasteurella multocida.

Pasteurella multocida toxin is a potent mitogen that is believed to act intracellularly. On transverse urea gradient gels at pH 8.0 the toxin displayed one major unfolding transition at 4 M urea. However, at pH 6.1 the unfolding transition took place at 3.5 M urea. Circular dichroism spectra also indicated that a structural change took place at acidic pH. In addition it was found that the toxin that had been denatured in 8 M urea refolded in solution with a high recovery of biological activity. These findings are discussed in terms of the likely domain structure of the P. multocida toxin.

3T3 Cells↗

PubMed2006

Structural changes of alpha-lactalbumin induced by low pH and oleic acid.

The effects of low pH and oleic acid on conformation and association state of Ca2+-depleted bovine alpha-lactalbumin (apo-BLA) have been studied by electrospray ionization mass spectrometry, fluorescence spectroscopy, and circular dichroism. The experimental results demonstrate that two structurally distinct species exist in the conformational transition of apo-BLA induced by low pH. One species populates at pH 3.0 characterized as a monomeric molten globule state and the other accumulates at pH 4.0-4.5 which is a partially folded dimer. Oleic acid promotes the formation of the dimeric intermediate at pH 4.0 and 7.0, but increases the content of molten globule state remarkably at pH 3.0 compared with that in the absence of oleic acid, indicating that oleic acid at pH 3.0 plays a different role from those at pH 4.0 and 7.0. Our data provide insight into the mechanism of pH-dependent and oleic acid-dependent structural changes and oligomerization of alpha-lactalbumin, and will be helpful to the understanding of the apoptosis-inducing function of multimeric alpha-lactalbumin in which oleic acid is a necessary cofactor.

Animals↗

PubMed2004

Structural changes in the photoactive site of proteorhodopsin during the primary photoreaction.

Proteorhodopsin (PR), found in marine gamma-proteobacteria, is a newly discovered light-driven proton pump similar to bacteriorhodopsin (BR). Because of the widespread distribution of proteobacteria in the worldwide oceanic waters, this pigment may contribute significantly to the global solar energy input in the biosphere. We examined structural changes that occur during the primary photoreaction (PR --> K) of wild-type pigment and two mutants using low-temperature FTIR difference spectroscopy. Several vibrations detected in the 3500-3700 cm(-1) region are assigned on the basis of H(2)O --> H(2)(18)O exchange to the perturbation of one or more internal water molecules. Substitution of the negatively charged Schiff base counterion, Asp97, with the neutral asparagine caused a downshift of the ethylenic (C=C) and Schiff base (C=N) stretching modes, in agreement with the 27 nm red shift of the visible lambda(max). However, this replacement did not alter the normal all-trans to 13-cis isomerization of the chromophore or the environment of the detected water molecule(s). In contrast, substitution of Asn230, which is in a position to interact with the Schiff base, with Ala induces a 5 nm red shift of the visible lambda(max) and alters the PR chromophore structure, its isomerization to K, and the environment of the detected internal water molecules. The combination of FTIR and site-directed mutagenesis establishes that both Asp97 and Asn230 are perturbed during the primary phototransition. The environment of Asn230 is further altered during the thermal decay of K. These results suggest that significant differences exist in the conformational changes which occur in the photoactive sites of proteorhodopsin and bacteriorhodopsin during the primary photoreaction.

Amino Acid Substitution↗

PubMed2005

Accumulation of amino acid substitutions promotes irreversible structural changes in the hemagglutinin of human influenza AH3 virus during evolution.

In order to clarify the effect of an accumulation of amino acid substitutions on the hemadsorption character of the influenza AH3 virus hemagglutinin (HA) protein, we introduced single-point amino acid changes into the HA1 domain of the HA proteins of influenza viruses isolated in 1968 (A/Aichi/2/68) and 1997 (A/Sydney/5/97) by using PCR-based random mutation or site-directed mutagenesis. These substitutions were classified as positive or negative according to their effects on the hemadsorption activity. The rate of positive substitutions was about 50% for both strains. Of 44 amino acid changes that were identical in the two strains with regard to both the substituted amino acids and their positions in the HA1 domain, 22% of the changes that were positive in A/Aichi/2/68 were negative in A/Sydney/5/97 and 27% of the changes that were negative in A/Aichi/2/68 were positive in A/Sydney/5/97. A similar discordance rate was also seen for the antigenic sites. These results suggest that the accumulation of amino acid substitutions in the HA protein during evolution promoted irreversible structural changes and therefore that antigenic changes in the H3HA protein may not be limited.

Amino Acid Sequence↗

PubMed1978

Structural changes of ribosome by the action of ethylene glycol.

The denaturation of ribosome and RNA by ethylene glycol (EG) has been studied in an attempt to further understand the conformation and stability of the ribosome. At high concentrations of EG, the ribosome, its subunits, and 16S RNA undergo drastic structural changes as shown by circular dichroism, ultraviolet absorption spectroscopy, and sedimentation velocity. Two separate conformational transitions were observed for the 30S subunit; one from 30 to 50% EG and another from 60 to 90% EG. This observation suggests the presence of two "domains" in the 30S subunit which differ in their stability. However, the 50S subunit undergoes a single sharp transition at 60 to 90% EG, consistent with the notion of a highly cooperative conformation. Association of the subunits stablizes part of the 30S subunit since the transition curve for the 70S ribosome does not exhibit significant change at the low EG concentration region as seen for the 30S subunit. Removal of proteins from the 30S subunit broadens the transition curve to lower EG concentrations and suggests the role of proteins in stabilizing the conformation of the 16S RNA.

Cell Fractionation↗

PubMed1999

Phosphorylation-dependent structural changes in the regulatory light chain domain of smooth muscle heavy meromyosin.

Smooth muscle heavy meromyosin, a double-headed proteolytic fragment of myosin lacking the COOH-terminal two-thirds of the tail, has been shown previously to be regulated by phosphorylation. To examine phosphorylation-dependent structural changes near the head-tail junction, we prepared five well regulated heavy meromyosins containing single-cysteine mutants of the human smooth muscle regulatory light chain labeled with the photocross-linking reagent, benzophenone-iodoacetamide. For those mutants that generated cross-links, only one type of cross-linked species was observed, a regulatory light chain dimer. Irradiated mutants fell into two classes. First, for Q15C, A23C, and wild type (Cys-108), a regulatory light chain dimer was formed for dephosphorylated but not thiophosphorylated heavy meromyosin. These data provide direct chemical evidence that in the dephosphorylated state, Gln-15, Ala-23, and Cys-108 on one head are positioned near (within 8.9 A) the regulatory light chain of the partner head and that thiophosphorylation abolishes proximity. This behavior was also observed for the Q15C mutant on a truncated heavy meromyosin lacking both catalytic domains. For the actin-heavy meromyosin complex, cross-links were formed in both de- and thiophosphorylated states. S59C and T134C mutants were in a second mutant class, where regulatory light chain dimers were not detected in dephosphorylated or thiophosphorylated heavy meromyosin, suggesting positions outside the region of interaction of the regulatory light chains.

Amino Acid Sequence↗

PubMed2002

Membrane structural changes support the involvement of mitochondria in the bile salt-induced apoptosis of rat hepatocytes.

The accumulation of toxic bile salts within the hepatocyte plays a key role in organ injury during liver disease. Deoxycholate (DC) and glycochenodeoxycholate (GCDC) induce apoptosis in vitro and in vivo, perhaps through direct perturbation of mitochondrial membrane structure and function. In contrast, ursodeoxycholate (UDC) and its taurine-conjugated form (TUDC) appear to be protective. We show here that hydrophobic bile salts induced apoptosis in cultured rat hepatocytes, without modulating the expression of pro-apoptotic Bax protein, and caused cytochrome c release in isolated mitochondria. Co-incubation with UDC and TUDC prevented cell death and efflux of mitochondrial factors. Using spin-labelling techniques and EPR spectroscopy analysis of isolated rat liver mitochondria, we found significant structural changes at the membrane-water surface in mitochondria exposed to hydrophobic bile salts, including modified lipid polarity and fluidity, altered protein order and increased oxidative injury. UDC, TUDC and cyclosporin A almost completely abrogated DC- and GCDC-induced membrane perturbations. We conclude that the toxicity of hydrophobic bile salts to hepatocytes is mediated by cytochrome c release, through a mechanism associated with marked direct effects on mitochondrial membrane lipid polarity and fluidity, protein order and redox status, without modulation of pro-apoptotic Bax expression. UDC and TUDC can directly suppress disruption of mitochondrial membrane structure, which may represent an important mechanism of hepatoprotection by these bile salts.

Animals↗

PubMed2003

Assembly of protein subunits within the stromal ridge of photosystem I. Structural changes between unbound and sequentially PS I-bound polypeptides and correlated changes of the magnetic properties of the terminal iron sulfur clusters.

The X-ray structure of Photosystem I (PS I) from Synechococcus elongatus was recently solved at 2.5A resolution (PDB entry 1JB0). It provides a structural model for the stromal subunits PsaC, PsaD and PsaE, which comprise the "stromal ridge" of PS I. In a separate set of studies the three-dimensional solution structures of the unbound, recombinant PsaC (PDB entry 1K0T) and PsaE (PDB entries 1PSF, 1QP2 and 1GXI) subunits were solved by NMR. The PsaC subunit of PS I is a small (9.3 kDa) protein that harbors binding sites for two [4Fe-4S] clusters F(A) and F(B), which are the terminal electron acceptors in PS I. Comparison of the PsaC structure in solution with that in the X-ray structure of PS I reveals significant differences between them which are summarized and evaluated here. Changes in the magnetic properties of [4Fe-4S] centers F(A) and F(B) are related to changes in the protein structure of PsaC, and they are further influenced by the presence of PsaD. Based on experimental evidence, three assembly stages are analyzed: PsaC(free), PsaC(only), PsaC(PS I). Unbound, recombinant PsaD, studied by NMR, has only a few elements of secondary structure and no stable three-dimensional structure in solution. When PsaD is bound in PS I, it has a well-defined three-dimensional structure. For PsaE the three-dimensional structure is very similar in solution and in the PS I-bound form, with the exception of two loop regions. We suggest that the changes in the structures of PsaC and PsaD are caused by the sequential formation of multiple networks of contacts between the polypeptides of the stromal ridge and between those polypeptides and the PsaA/PsaB core polypeptides. The three-dimensional structure of the C(2)-symmetric F(X)-binding loops on PsaA and PsaB were also analyzed and found to be significantly different from the binding sites of other proteins that contain interpolypeptide [4Fe-4S] clusters. The aim of this work is to relate contact information to structural changes in the proteins and to propose a model for the assembly of the stromal ridge of PS I based on this analysis.

Amino Acid Motifs↗

PubMed1990

Structural changes in the ribosomal genes of immortalized and transformed mouse embryo C3H/10T1/2 cell lines.

Comparative studies of DNA isolated from adult C3H mouse liver, immortalized mouse embryo cells (C3H/10T1/2 Cl 8) and the tumorigenic methylcholanthrene transformed C3H/10T1/2 Cl 16 cell line have been carried out in order to analyze possible structural changes in the ribosomal genes associated with the immortalization and tumorigenic transformation of mouse cells. Southern blot hybridization experiments revealed a mutation hotspot within repetitive sequences 13 kb upstream from the 18S rRNA genes in the non-transcribed spacer (NTS). Other DNA changes were localized near the initiation and termination regions of rRNA transcription. The differences found in the restriction maps of the 5'-region resided 5 to 6 kd upstream from the 18S 5'-end and the changes located in the 3'-end mapped approximately 5 kb downstream from the 28S 3'-end. Thus, oncogenic transformation of the C3H/10T1/2 Cl 8 cells by methylcholanthrene treatment was associated with stable genetic changes in the 18S rRNA gene. There was no evidence for rRNA gene amplification.

Animals↗