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Solvent Conditions (solvent + condition)

Distribution by Scientific Domains

Chemistry	80%

Selected Abstracts

Preparation of a sorbitol methacrylate grafted silica as stationary phase for hydrophilic interaction chromatography

JOURNAL OF SEPARATION SCIENCE, JSS, Issue 9 2008
Jonas Persson
Abstract A new highly hydrophilic stationary phase based on graft polymerization of sorbitol methacrylate from the surface of Kromasil silica particles is described. Polymerization was initiated by thermal cleavage of tert -butyl hydroperoxide covalently attached to the silica particle surface. Due to the highly amphiphilic properties of the monomer, an extensive search was needed to find solvent conditions that enabled surface-initiated polymerization. This was finally solved by using a mixture of solvents that only partially dissolved the monomer. The graft polymerization was confirmed by Fourier transform infrared spectroscopy and elemental analysis. The resulting stationary phase was evaluated by HPLC and exhibited a selectivity markedly different from that of commercially available columns and of neat silica. [source]

Grafted Polymer Chains Interacting with Substrates: Computer Simulations and Scaling

MACROMOLECULAR THEORY AND SIMULATIONS, Issue 9 2008
Radu Descas
Abstract We review scaling methods and computer simulations used in the study of the static and dynamic properties of polymer chains tethered to adsorbing surfaces under good solvent conditions. By varying both the grafting density and the monomer/surface interactions a variety of phases can form. In particular, for attractive interactions between the chains and the surface the classical mushroom-brush transition known for repulsive substrates splits up into an overlap transition and a saturation transition which enclose a region of semidilute surface states. At high grafting densities oversaturation effects and a transition to a brush state can occur. We emphasize the role of the critical adsorption parameters for a correct description and understanding of such polymer adsorption phenomena. [source]

One- and Two-Component Bottle-Brush Polymers: Simulations Compared to Theoretical Predictions

MACROMOLECULAR THEORY AND SIMULATIONS, Issue 7 2007
Hsiao-Ping Hsu
Abstract Scaling predictions for bottle-brush polymers with a rigid backbone and flexible side chains under good solvent conditions are discussed and their validity is assessed by a comparison with Monte Carlo simulations of a simple lattice model. It is shown that typically only a rather weak stretching of the side chains is realized, and then the scaling predictions are not applicable. Also two-component bottle brush polymers are considered, where two types (A,B) of side chains are grafted, assuming that monomers of different kind repel each other. In this case, variable solvent quality is allowed. Theories predict "Janus cylinder"-type phase separation along the backbone in this case. The Monte Carlo simulations, using the pruned-enriched Rosenbluth method (PERM) give evidence that the phase separation between an A-rich part of the cylindrical molecule and a B-rich part can only occur locally. The correlation length of this microphase separation can be controlled by the solvent quality. This lack of a phase transition is interpreted by an analogy with models for ferromagnets in one space dimension. [source]

Amyloid,a state in many guises: Survival of the fittest fibril fold

PROTEIN SCIENCE, Issue 1 2008
Jesper S. Pedersen
Abstract Under appropriate conditions, essentially all proteins are able to aggregate to form long, well-ordered and ,-sheet-rich arrays known as amyloid-like fibrils. These fibrils consist of varying numbers of intertwined protofibrils and can for any given protein exhibit a wealth of different forms at the ultrastructural level. Traditionally, this structural variability or polymorphism has been attributed to differences in the assembly of a common protofibril structure. However, recent work on glucagon, insulin, and the A, peptide suggests that this polymorphism can occur at the level of secondary structure. Simple variations in either solvent conditions such as temperature, protein concentration, and ionic strength or external mechanical influences such as agitation can lead to formation of fibrils with markedly different characteristics. In some cases, these characteristics can be passed on to new fibrils in a strain-specific manner, similar to what is known for prions. The preferred structure of fibrils formed can be explained in terms of selective pressure and survival of the fittest; the most populated types of fibrils we observe at the end of an experiment are those that had the fastest overall growth rate under the given conditions. Fibrillar polymorphism is probably a consequence of the lack of structural restraints on a nonfunctional conformational state. [source]

Detecting equilibrium cytochrome c folding intermediates by electrospray ionisation mass spectrometry: Two partially folded forms populate the molten-globule state

PROTEIN SCIENCE, Issue 3 2002
Rita Grandori
Abstract Nanoelectrospray ionization mass spectrometry (nano-ESI-MS) is applied to the characterization of ferric cytochromec (cytc) conformational states under different solvent conditions. The methanol-induced molten-globule state in the pH range 2.6,3.0 is found to be populated by two distinct, partially folded conformers IA and IB. The more compact intermediate IB resembles that induced by glycerol in acid-unfolded cytc. The less compact one, IA, also can be induced by destabilization of the native structure by trifluoroethanol. IA and IB can be detected, in the absence of additives, around the midpoint of the acid-induced unfolding transition, providing direct evidence for involvement of equilibrium folding intermediates in cytc conformational transitions at low pH. This study shows that mass spectrometry can contribute to the characterization of molten-globule states of proteins by detection of distinct, although poorly populated, conformations involved in a dynamic equilibrium. [source]

Mimicry of dimerization by synthetic peptides designed to target homologous regions of proteins

PROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 3 2003
Donard S. Dwyer
Abstract Rapid progress in sequencing various genomes has highlighted the need for the development of biochemical reagents for the detection of thousands of expressed gene products. The magnitude of this detection problem exceeds current technical capabilities. In an attempt to address this shortcoming, a novel approach has been developed called mimicry of dimerization. Peptide tags have been designed to bind to a specific region of parvalbumin on the basis of amino acid sequence homology with this segment. Multivalent ligands were produced by coupling the synthetic peptides to activated dextran polymers and binding was assessed by chemiluminescence of enhanced avidity reactions using a high density of target protein at the binding surface. Binding of the peptide ligands to parvalbumin was strongest under assay conditions that enriched for native monomeric protein and was affected by pH, temperature and solvent conditions. The results suggest that it should be possible to develop specific reagents for tagging proteins on the basis of sequence and secondary structure information. [source]

Travelling wave ion mobility mass spectrometry studies of protein structure: biological significance and comparison with X-ray crystallography and nuclear magnetic resonance spectroscopy measurements

RAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 20 2008
Charlotte A. Scarff
The three-dimensional conformation of a protein is central to its biological function. The characterisation of aspects of three-dimensional protein structure by mass spectrometry is an area of much interest as the gas-phase conformation, in many instances, can be related to that of the solution phase. Travelling wave ion mobility mass spectrometry (TWIMS) was used to investigate the biological significance of gas-phase protein structure. Protein standards were analysed by TWIMS under denaturing and near-physiological solvent conditions and cross-sections estimated for the charge states observed. Estimates of collision cross-sections were obtained with reference to known standards with published cross-sections. Estimated cross-sections were compared with values from published X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy structures. The cross-section measured by ion mobility mass spectrometry varies with charge state, allowing the unfolding transition of proteins in the gas phase to be studied. Cross-sections estimated experimentally for proteins studied, for charge states most indicative of native structure, are in good agreement with measurements calculated from published X-ray and NMR structures. The relative stability of gas-phase structures has been investigated, for the proteins studied, based on their change in cross-section with increase in charge. These results illustrate that the TWIMS approach can provide data on three-dimensional protein structures of biological relevance. Copyright © 2008 John Wiley & Sons, Ltd. [source]

Terahertz time-domain spectroscopy of poly- L -lysine

BIOPOLYMERS, Issue 8 2010
Ohki Kambara
Abstract Poly- L -lysine is known to have three different secondary structures depending on solvent conditions because of its flexible nature. In previous work (Kambara et al., Phys Chem Chem Phys 2008, 10, 5042-5044), we observed two different types of structural changes in poly- L -lysine. In the present study, we investigated the low-frequency spectrum of poly- L -lysine with a ,-sheet structure in the solid state by terahertz time-domain spectroscopy. On the basis of this spectroscopic analysis, we found that the low-frequency dynamics differed from those of other polypeptides. Furthermore, we performed powder X-ray diffraction measurement on poly- L -lysine, which was found to be highly amorphous compared with other polypeptides. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 735,739, 2010. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source]

Preliminary structural investigations of the Eut-L shell protein of the ethanolamine ammonia-lyase metabolosome of Escherichia coli

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 2 2009
Kiel Nikolakakis
The ethanolamine ammonia-lyase microcompartment is composed of five different shell proteins that have been proposed to assemble into symmetrically shaped polyhedral particles of varying sizes. Here, preliminary X-ray analysis of crystals of the bacterial microcompartment shell protein Eut-L from Escherichia coli is reported. Cloning, overexpression and purification resulted in highly pure protein that crystallized readily under many different conditions. In all cases the protein forms thin hexagonal plate-shaped crystals belonging to space group P3 that are of unusually high stability against different solvent conditions. The crystals diffracted to a resolution of 2.0,Å using synchrotron radiation but proved to be radiation-sensitive. Preparations of heavy-atom-derivatized crystals for use in determining the three-dimensional structure are under way. [source]

DNA Condensation by Field-Induced Non-Equilibrium Noise

CHEMPHYSCHEM, Issue 16 2009
Robijn F. Bruinsma Prof.
Abstract DNA molecules under good solvent conditions condense when subjected to strong AC electrical fields. It is shown that AC electrical fields couple charge fluctuations to molecular shape fluctuations, which produces a non-equilibrium noise source that can dominate over equilibrium thermal noise in the long-wavelength limit. The field-induced excess charge fluctuations amplify the Asakura,Oosawa fluctuation attraction force between neighboring chains, providing a mechanism for field-induced DNA condensation. [source]