Effect of SDS on human hair: Study on the molecular structure and morphology

This paper presents a model study to understand the effect of surfactants on the physicochemical properties of human hair. FT-IR ATR spectroscopy has been employed to understand the chemical changes induced by sodium dodecyl sulfate (SDS) on human scalp hair. In particular, the SDS induced changes in the secondary structure of protein present in the outer protective layer of hair, i.e. cuticle, have been investigated. Conformational changes in the secondary structure of protein were studied by curve fitting of the amide I band after every phase of SDS treatment. It has been found that SDS brings rearrangements in the protein backbone conformations by transforming beta-sheet structure to random coil and beta-turn. Additionally, AFM and SEM studies were carried out to understand the morphological changes induced on the hair surface. SEM and AFM images demonstrated the rupture and partial erosion of cuticle sublayers.

Singularity structure of third-order dynamical systems .2

The singularity structure of the solutions of a general third-order system, with polynomial right-hand sides of degree less than or equal to two, is studied about a movable singular point, An algorithm for transforming the given third-order system to a third-order Briot-Bouquet system is presented, The dominant behavior of a solution of the given system near a movable singularity is used to construct a transformation that changes the given system directly to a third-order Briot-Bouquet system. The results of Horn for the third-order Briot-Bouquet system are exploited to give the complete form of the series solutions of the given third-order system; convergence of these series in a deleted neighborhood of the singularity is ensured, This algorithm is used to study the singularity structure of the solutions of the Lorenz system, the Rikitake system, the three-wave interaction problem, the Rabinovich system, the Lotka-Volterra system, and the May-Leonard system for different sets of parameter values. The proposed approach goes far beyond the ARS algorithm.

Molybdenum tetracarbonyl complexes of (aryloxy) lambda(3)-cyclotriphosphazanes; X-ray crystal structure of [Mo(CO)(4){EtNP(OC6H4Br-4)}(3)]

Treatment of the lambda(3)-cyclotriphosphazanes, cis-{EtNP(OR)}(3) [R = C6H4Br-4 (L-1) or C6H4Br-2 (L-2)] with [Mo(CO)(4)(NBD)] (NBD = norbornadiene) yields the mononuclear complexes [Mo(CO)(4)L-1] (1) and [Mo(CO)(4)L-2] (2). which have been characterised by IR, NMR (P-31 and H-1) and FAB mass spectral data. The structure of 1 has been confirmed by single crystal X-ray analysis. The structural and conformational changes brought about by complexation are discussed in terms of a bonding model based on "negative hyperconjugation". (C) 1998 Elsevier Science Ltd. All rights reserved.

Structure of basic winged-bean lectin and a comparison with its saccharide-bound form

The crystal structure of the saccharide-free form of the basic form of winged-bean agglutinin (WBAI) has been solved by the molecular-replacement method and refined at 2.3 Angstrom resolution The final R factor is 19.74b for all data in the resolution range 8.0-2.3 Angstrom. The asymmetric unit contains two half-dimers, each located on a crystallographic twofold axis. The structure of the saccharide-free form is compared with that of the complex of WBAI wi th methyl-alpha-D-galactoside. The complex is composed of two dimers in the asymmetric unit. The intersubunit interactions in the dimer are nearly identical in the two structures The binding site of the saccharide-free structure contains three ordered water molecules at positions similar to those of the hydroxyl groups of the carbohydrate which an hydrogen bonded to the protein. Superposition of the saccharide-binding sites of the two structures shows that the major changes involve expulsion of these ordered water molecules and a shift of about 0.6 Angstrom of the main-chain atoms of the variable loop.

Vertical thermal structure of the atmosphere during active and weak phases of convection over the north Bay of Bengal: Observation and model results

Owing to the lack of atmospheric vertical profile data with sufficient accuracy and vertical resolution, the response of the deep atmosphere to passage of monsoon systems over the Bay of Bengal. had not been satisfactorily elucidated. Under the Indian Climate Research Programme, a special observational programme called 'Bay of Bengal Monsoon Experiment' (BOBMEX), was conducted during July-August 1999. The present study is based on the high-resolution radiosondes launched during BOBMEX in the north Bay. Clear changes in the vertical thermal structure of the atmosphere between active and weak phases of convection have been observed. The atmosphere cooled below 6 km height and became warmer between 6 and 13 km height. The warmest layer was located between 8 and 10 km height, and the coldest layer was found just below 5 km height. The largest fluctuations in the humidity field occurred in the mid-troposphere. The observed changes between active and weak phases of convection are compared with the results from an atmospheric general circulation model, which is similar to that used at the National Centre for Medium Range Weather Forecasting, New Delhi. The model is not able to capture realistically some important features of the temperature and humidity profiles in the lower troposphere and in the boundary layer during the active and weak spells.

Structure and nucleotide specificity of Staphylococcus aureus dihydrodipicolinate reductase (DapB)

Lysine biosynthesis proceeds by the nucleotide-dependent reduction of dihydrodipicolinate (DHDP) to tetrahydrodipicolinate (THDP) by dihydrodipicolinate reductase (DHDPR). The S. aureus DHDPR structure reveals different conformational states of this enzyme even in the absence of a substrate or nucleotide-cofactor. Despite lacking a conserved basic residue essential for NADPH interaction, S. aureus DHDPR differs from other homologues as NADPH is a more preferred co-factor than NADH. The structure provides a rationale-Lys35 compensates for the co-factor site mutation. These observations are significant for bi-ligand inhibitor design that relies on ligand-induced conformational changes as well as co-factor specificity for this important drug target. Structured summary of protein interactions: DHDPR binds to DHDPR by molecular sieving (View interaction). DHDPR binds to DHDPR by dynamic light scattering (View interaction). DHDPR binds to DHDPR by X-ray crystallography (View interaction). (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Conformational basis for substrate recognition and regulation of catalytic activity in Staphylococcus aureus nucleoside di-phosphate kinase

Nucleoside diphosphate kinases (NDK) are characterized by high catalytic turnover rates and diverse substrate specificity. These features make this enzyme an effective activator of a pro-drug an application that has been actively pursued for a variety of therapeutic strategies. The catalytic mechanism of this enzyme is governed by a conserved histidine that coordinates a magnesium ion at the active site. Despite substantial structural and biochemical information on NDK, the mechanistic feature of the phospho-transfer that leads to auto-phosphorylation remains unclear. While the role of the histidine residue is well documented, the other active site residues, in particular the conserved serine remains poorly characterized. Studies on some homologues suggest no role for the serine residue at the active site, while others suggest a crucial role for this serine in the regulation and quaternary association of this enzyme in some species. Here we report the biochemical features of the Staphylococcus aureus NDK and the mutant enzymes. We also describe the crystal structures of the apo-NDK, as a transition state mimic with vanadate and in complex with different nucleotide substrates. These structures formed the basis for molecular dynamics simulations to understand the broad substrate specificity of this enzyme and the role of active site residues in the phospho-transfer mechanism and oligomerization. Put together, these data suggest that concerted changes in the conformation of specific residues facilitate the stabilization of nucleotide complexes thereby enabling the steps involved in the ping-pong reaction mechanism without large changes to the overall structure of this enzyme. (C) 2011 Elsevier B.V. All rights reserved.

Conformational changes of the chaperone SecB upon binding to a model substrate - bovine pancreatic trypsin inhibitor (BPTI)

SecB is a homotetrameric cytosolic chaperone that forms part of the protein translocation machinery in E. coli. Due to SecB, nascent polypeptides are maintained in an unfolded translocation-competent state devoid of tertiary structure and thus are guided to the translocon. In vitro SecB rapidly binds to a variety of ligands in a non-native state. We have previously investigated the bound state conformation of the model substrate bovine pancreatic trypsin inhibitor (BPTI) as well as the conformation of SecB itself by using proximity relationships based on site-directed spin labeling and pyrene fluorescence methods. It was shown that SecB undergoes a conformational change during the process of substrate binding. Here, we generated SecB mutants containing but a single cysteine per subunit or an exposed highly reactive new cysteine after removal of the nearby intrinsic cysteines. Quantitative spin labeling was achieved with the methanethiosulfonate spin label (MTS) at positions C97 or E90C, respectively. Highfield (W-band) electron paramagnetic resonance (EPR) measurements revealed that with BPTI present the spin labels are exposed to a more polar/hydrophilic environment. Nanoscale distance measurements with double electron-electron resonance (DEER) were in excellent agreement with distances obtained by molecular modeling. Binding of BPTI also led to a slight change in distances between labels at C97 but not at E90C. While the shorter distance in the tetramer increased, the larger diagonal distance decreased. These findings can be explained by a widening of the tetrameric structure upon substrate binding much like the opening of two pairs of scissors.

Structure of tandem and its implication for bifunctional intercalation into dna

Quinoxaline antibiotics (Fig. 1a, b) form a useful group of compounds for the study of drug–nucleic acid interactions1,2. They consist of a cross-bridged cyclic octadepsipeptide, variously modified, bearing two quinoxaline chromophores. These antibiotics intercalate bifunctionally into DNA2,3 probably via the narrow groove, forming a complex in which, most probably, two base pairs are sandwiched between the chromophores4,5. Depending on the nature of their sulphur-containing cross-bridge and modifications to their amino acid side chains, they display characteristic patterns of nucleotide sequence selectivity when binding to DNAs of different base composition and to synthetic polydeoxynucleotides4,6,7. This specificity has been tentatively ascribed to specific hydrogen-bonding interactions between functional groups in the DNA and complementary moieties on the peptide ring2,4,5. Variations in selectivity have been attributed both to changes in the conformation of the peptide backbone6 and no modifications of the cross-bridge7. These suggestions were made, however, in the absence of firm knowledge about the three-dimensional structure and conformation of the antibiotic molecules. We now report the X-ray structure analysis of the synthetic analogue of the antibiotic triostin A, TANDEM (des-N-tetramethyl triostin A) (Fig. 1c), which binds preferentially to alternating adenine-thymine sequences7. The X-ray structure provides a starting point for exploring the origin of this specificity and suggests possible models for the binding of other members of the quinoxaline series.

Structure and morphology studies of chromium film at elevated temperature in hypersonic environment

This paper presents the after shock heated structural and morphological studies of chromium film coated on hypersonic test model as a passive drag reduction element. The structural changes and the composition of phases of chromium due to shock heating (2850 K) are characterized using X-ray diffraction studies. Surface morphology changes of chromium coating have been studied using scanning electron microscopy (SEM) before and after shock heating. Significant amount of chromium ablation and sublimation from the model surface is noticed from SEM micrographs. Traces of randomly oriented chromium oxides formed along the coated surface confirm surface reaction of chromium with oxygen present behind the shock. Large traces of amorphous chromium oxide phases are also observed.

Dramatic Structural Changes Resulting from the Loss of a Crucial Hydrogen Bond in the Hinge Region Involved in C-Terminal Helix Swapping in SurE: A Survival Protein from Salmonella typhimurium

Domain swapping is an interesting feature of some oligomeric proteins in which each protomer of the oligomer provides an identical surface for exclusive interaction with a segment or domain belonging to another protomer. Here we report results of mutagenesis experiments on the structure of C-terminal helix swapped dimer of a stationary phase survival protein from Salmonella typhimurium (StSurE). Wild type StSurE is a dimer in which a large helical segment at the C-terminus and a tetramerization loop comprising two beta strands are swapped between the protomers. Key residues in StSurE that might promote C-terminal helix swapping were identified by sequence and structural comparisons. Three mutants in which the helix swapping is likely to be avoided were constructed and expressed in E. coli. Three-dimensional X-ray crystal structures of the mutants H234A and D230A/H234A could be determined at 2.1 angstrom and 2.35 angstrom resolutions, respectively. Contrary to expectations, helix swapping was mostly retained in both the mutants. The loss of the crucial D230 OD2- H234 NE2 hydrogen bond (2.89 angstrom in the wild type structure) in the hinge region was compensated by new inter and intra-chain interactions. However, the two fold molecular symmetry was lost and there were large conformational changes throughout the polypeptide. In spite of these changes, the dimeric structure and an approximate tetrameric organization were retained, probably due to the interactions involving the tetramerization loop. Mutants were mostly functionally inactive, highlighting the importance of precise inter-subunit interactions for the symmetry and function of StSurE.

Insight into morphology changes of nanoparticle laden droplets in acoustic field

Hollow structures with unique morphologies form due to particle agglomeration in acoustically levitated nanofluid functional droplets when subjected to external heating. The final diameter of the structure depends only on the ratio of agglomeration to evaporation time scales for various nanoparticle laden droplets, and not on the type of the suspended particles. These time scales depend only on nanoparticle concentration. This valuable information may be exploited to form microstructures with desired properties from ceramic compounds. Phase diagrams for alumina and silica droplets indicate the transition from a bowl to ring structure depending on concentration.

Solution nuclear magnetic resonance structure of the GATase subunit and structural Basis of the interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from methanocaldococcus jannaschii

The solution structure of the monomeric glutamine amidotransferase (GATase) subunit of the Methanocaldococcus janaschii (Mj) guanosine monophosphate synthetase (GMPS) has been determined using high-resolution nuclear magnetic resonance methods. Gel filtration chromatography and N-15 backbone relaxation studies have shown that the Mj GATase subunit is present in solution as a 21 kDa (188-residue) monomer. The ensemble of 20 lowest-energy structures showed root-mean-square deviations of 0.35 +/- 0.06 angstrom for backbone atoms and 0.8 +/- 0.06 angstrom for all heavy atoms. Furthermore, 99.4% of the backbone dihedral angles are present in the allowed region of the Ramachandran map, indicating the stereochemical quality of the structure. The core of the tertiary structure of the GATase is composed of a seven-stranded mixed beta-sheet that is fenced by five alpha-helices. The Mj GATase is similar in structure to the Pyrococcus horikoshi (Ph) GATase subunit. Nuclear magnetic resonance (NMR) chemical shift perturbations and changes in line width were monitored to identify residues on GATase that were responsible for interaction with magnesium and the ATPPase subunit, respectively. These interaction studies showed that a common surface exists for the metal ion binding as well as for the protein-protein interaction. The dissociation constant for the GATase-Mg2+ interaction has been found to be similar to 1 mM, which implies that interaction is very weak and falls in the fast chemical exchange regime. The GATase-ATPPase interaction, on the other hand, falls in the intermediate chemical exchange regime on the NMR time scale. The implication of this interaction in terms of the regulation of the GATase activity of holo GMPS is discussed.

The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs

The sequence and structure of snake gourd seed lectin (SGSL), a nontoxic homologue of type II ribosome-inactivating proteins (RIPs), have been determined by mass spectrometry and X-ray crystallography, respectively. As in type II RIPs, the molecule consists of a lectin chain made up of two beta-trefoil domains. The catalytic chain, which is connected through a disulfide bridge to the lectin chain in type II RIPs, is cleaved into two in SGSL. However, the integrity of the three-dimensional structure of the catalytic component of the molecule is preserved. This is the first time that a three-chain RIP or RIP homologue has been observed. A thorough examination of the sequence and structure of the protein and of its interactions with the bound methyl-alpha-galactose indicate that the nontoxicity of SGSL results from a combination of changes in the catalytic and the carbohydrate-binding sites. Detailed analyses of the sequences of type II RIPs of known structure and their homologues with unknown structure provide valuable insights into the evolution of this class of proteins. They also indicate some variability in carbohydrate-binding sites, which appears to contribute to the different levels of toxicity exhibited by lectins from various sources.

Elastic thickness structure of the Andaman subduction zone: Implications for convergence of the Ninetyeast Ridge

We use the Bouguer coherence (Morlet isostatic response function) technique to compute the spatial variation of effective elastic thickness (T-e) of the Andaman subduction zone. The recovered T-e map resolves regional-scale features that correlate well with known surface structures of the subducting Indian plate and the overriding Burma plate. The major structure on the India plate, the Ninetyeast Ridge (NER), exhibits a weak mechanical strength, which is consistent with the expected signature of an oceanic ridge of hotspot origin. However, a markedly low strength (0< T-e <3 km) in that region, where the NER is close to the Andaman trench (north of 10 N), receives our main attention in this study. The subduction geometry derived from the Bouguer gravity forward modeling suggests that the NER has indented beneath the Andaman arc. We infer that the bending stresses of the viscous plate, which were reinforced within the subducting oceanic plate as a result of the partial subduction of the NER buoyant load, have reduced the lithospheric strength. The correlation, T-e < T-s (seismogenic thickness) reveals that the upper crust is actively deforming beneath the frontal arc Andaman region. The occurrence of normal-fault earthquakes in the frontal arc, low Te zone, is indicative of structural heterogeneities within the subducting plate. The fact that the NER along with its buoyant root is subducting under the Andaman region is inhibiting the subduction processes, as suggested by the changes in trench line, interrupted back-arc volcanism, variation in seismicity mechanism, slow subduction, etc. The low T-e and thinned crustal structure of the Andaman back-arc basin are attributed to a thermomechanically weakened lithosphere. The present study reveals that the ongoing back-arc spreading and strike-slip motion along the West Andaman Fault coupled with the ridge subduction exerts an important control on the frequency and magnitude of seismicity in the Andaman region. (C) 2013 Elsevier Ltd. All rights reserved.