Anatomical repair of exstrophy bladder.

An anatomical repair of bladder exstrophy was done in ten patients (six females and four males, aged 1.5-6 months. We describe our method of exstrophy with epispadias repair done in a single stage achieving anatomical closure including relocating skin from an infraphallic to a supraphallic position.

Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins.

Several recombinant proteins in inclusion bodies expressed in Escherichia coli have been measured by Fourier transform infrared and solid-state nuclear magnetic resonance spectra to provide the secondary structural characteristics of the proteins from hyperthermophilic archaeon Pyrococcus horikoshii OT3 (hyperthermophilic proteins) in inclusion bodies. The beta-strand-rich single chain Fv fragment (scFv) and alpha-helix-rich interleukin (IL)-4 lost part of the native-like secondary structure in inclusion bodies, while the inclusion bodies composed of the hyperthermophilic proteins of which the native form is alpha-helix rich, are predominated by alpha-helix structure. Further, the secondary structure of the recombinant proteins solubilized from inclusion bodies by detergent or denaturant was observed by circular dichroism (CD) spectra.

Adult onset celiac disease in north India.

Introduction: Informations on celiac disease among Indian adults is scarce. With the availability of improved and more accessible diagnostic tools for celiac disease, the disease is being more frequently recognized among the adults. Therefore, a retrospective analysis of duodenal biopsies were performed to identify adult celiac disease among Indian patients.

How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment.

The gradual removal of the denaturing reagent guanidine HCl (GdnHCl) using stepwise dialysis with the introduction of an oxidizing reagent and l-arginine resulted in the highly efficient refolding of various denatured single-chain Fv fragments (scFvs) from inclusion bodies expressed in Escherichia coli. In this study, the influence of the additives on the intermediates in scFv refolding was carefully analyzed on the basis of the stepwise dialysis, and it was revealed that the additive effect critically changes the pathway of scFv refolding. Circular dichroism and tryptophan fluorescence emission spectroscopies demonstrated that distinct secondary and tertiary structures were formed upon dialysis from 2 m GdnHCl to 1 m GdnHCl, and 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid dipotassium salt binding analysis indicated that the addition of l-arginine to the stepwise dialysis system effectively stabilized the exposed hydrophobic area on the scFv.

Folded conformation of an immunostimulating tetrapeptide rigin: high temperature molecular dynamics simulation study.

Employing high temperature quenched molecular dynamics (QMD) stimulations the conformational energy space of an immunostimulating tetrapeptide rigin: H-Gly341-Gln-Pro-Arg344-OH, is explored. Using distance dependent dielectric (epsilon =r(ij)) 31 different low energy starting structures with identical sequence were computed for their conformational preferences. According to the hypothesis of O'Connors et al.

Thermodynamics of hCG--monoclonal antibody interaction: an analysis of real time kinetics data obtained using radiolabeled hCG probe.

A thermodynamic analysis of the interaction of 125I-labeled human chorionic gonadotropin (IhCG) with two of its monoclonal antibodies (MAbs) was carried out. The dissociation profile of IhCG-MAb complex conforms to a two-step model. vant Hoff enthalpies were calculated with the K(A) (equilibrium constant) values obtained from dissociation at different temperatures.

Psammomatous extra-calvarial meningioma of the neck.

A case of Primary extraraniul meningioma of the parapharyngcal space arising simulitueouly as two distinct tumour masses from two sepurae cranial nerves is reported. The paucity of reported eases is the evidence for its rarily.

Visual detection of specific, native interactions between soluble and microbead-tethered alpha-helices from membrane proteins.

Using peptides tethered to polymer microbeads, we have developed a technique for measuring the interactions between the transmembrane alpha-helices of membrane proteins and for screening combinatorial libraries of peptides for members that interact with specific helices from membrane proteins. The method was developed using the well-characterized homodimerization sequence of the membrane-spanning alpha-helix from the erythrocyte membrane protein glycophorin A (GPA). As a control, we also tested a variant with a dimer-disrupting alteration of a critical glycine residue to leucine.

Characterization of a novel type VII beta-turn conformation for a bio-active tetrapeptide rigin A synergy between theoretical and experimental results.

The conformational analysis of an immunomodulating tetrapeptide rigin (H-Gly-Gln-Pro-Arg-OH), shown to possess diverse immunological activity, has been investigated both theoretically and experimentally for its conformational preferences. Unrestrained molecular dynamics simulation studies in implicit dimethylsulfoxide provide strong support for the existence of a significant population of ordered reverse turn structures for the major trans isomer. Of the three different energy minimized families, generated from computer molecular modelling, only one could be complemented by most of the 1D and 2D 1H NMR parameters obtained in dimethylsulfoxide-d6.

Theoretical study of conformational flexibility of tuftsin in vacuum and in aqueous environment.

Conformational flexibility of tuftsin molecule is studied using all-atom based atom-atom potential and systematic search, simulated annealing molecular dynamics (SAMD) and molecular dynamics (MD) techniques. Latter was carried out for 650 pico seconds (ps) using AMBER 4.0 with explicit water in TIP3P model.

Thermodynamic characterizations of an intramolecularly hydrogen bonded C5-structure across proteinogenic residue.

Thermodynamic investigations of a smallest possible intramolecularly hydrogen bonded C5-structure, across a Thr residue, in model peptides Boc-Xxx-Thr-NH2 (Xxx = Ile, 1 or Leu, 2), indicated unusual thermal stability of the structure in non-polar medium. An analysis of van't Hoff plots, constructed from variable temperature 1H NMR data, yielded the thermodynamic parameters of a hydrogen bonded five-membered ring. The non-significance of the spatial organizations of the preceding CdeltaH3 bearing hydrophobic proteinogenic residue on the thermal stability of the C5-structure has been observed.