Your search for structural biology returned 51 results
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19th Annual Conference of SBNet
Malvern is sponsoring the 19th Annual Conference of SBNet (Swedish Structural Biology Network) will take place at Åkerblads in Tällberg, on 12-15 of June.. . SBNet is the scientific network for Swedish structure biologists.. . Click here to access the full program . . We look forward to seeing you there!. .
Viruses of microbes Structure and function, from molecules to communities
The Viruses of microbes Structure and function, from molecules to communities, organized by the ETH Zurich will take place from 14th July to the 18th July 2014 at the ETH Zurich University in Zurich, Switzerland. The conference will cover areas like Viruses of microbes are the largest biological entity on planet earth, many aspects of the biology of viruses of microorganisms, the interaction with their hosts, and their ecological impact are not well understood and broad repertoire of tools which can be harnessed for a variety of applications in medicine..
Measurement type page
Understanding binding affinity is key to appreciation of the intermolecular interactions driving biological processes, structural biology, and structure-function relationships. It is also measured as part of the drug discovery process to help design drugs that bind their targets selectively and specifically..
An introduction to the bio-SAXS technique and its application on a versatile laboratory X-ray scattering platform
Webinar - Recorded
Webinar abstractPresented by: Joerg Bolze - Product Specialist X-ray Scattering Small-angle X-ray scattering (SAXS) applied to dilute protein solutions has become an accepted structural biology technique. In situ measurements provide information e.g. about protein size and shape, folding/unfolding, aggregation, stability and molecular weight. In this webinar we will give a basic introduction to the bio-SAXS technique, present Malvern Panalytical's SAXS instrumentaion (Empyrean Nano edition), and demonstrate its performance on a variety of protein samples. .
ScatterX78 for BioSAXS studies on dilute protein solutions
Performance validation against glucose isomeraseSmall-angle X-ray scattering from solutions of biological macromolecules, also known as BioSAXS, is a structural biology technique of rapidly increasing popularity. Other than with single crystal X-ray diffraction, SAXS allows to study proteins in their native state, dissolved in a suitable buffer, and crystallization is not required.Other than with single crystal X-ray diffraction, SAXS allows to study proteins in their native state, dissolved in a suitable buffer, and crystallization is not required. BioSAXS has proven as a valuable tool to analyze the overall size, compactness and aggregation behavior of protein molecules, and it can even be used to determine the 3D envelope structure at a resolution of 1-2 nm.. SAXS measurements were performed on a dilute solution of glucose isomerase. By using ScatterX78 experimental data could be acquired with good sensitivity and within short measurement times. The EasySAXS data analysis software was used to deduce information about the size, compactness, overall shape and aggregation behavior of the protein molecules. All results were found to be consistent and in good agreement with what has been reported in the scientific literature. .
Using Isothermal Titration Calorimetry to support the development of therapeutic enzymes
Webinar - Recorded
This webinar will describe the use of Isothermal Titration Calorimetry (ITC) to establish the enzymatic properties of a lysosomal enzyme with potential therapeutic value. The technique was used by the team at Swedish Orphan Biovitrum (Sobi) to enable the evaluation of multiple substrates, and to determine basic enzymatic characteristics. Dr. Stefan Svensson Gelius will describe how, in initial experiments, ITC enabled the demonstration of adhesion of the enzyme to surfaces, and later allowed confirmation of optimal buffer conditions. He will also discuss the problems the team encountered due to the polydispersity of a complex substrate mixture. The ITC methods developed at Sobi have been used to characterize batches and to establish structure-activity relationships supporting the development of the enzyme as a therapeutic molecule.
The power of powder - Screening of protein based pharmaceuticals
Webinar - Recorded
Proteins often form microcrystalline precipitates with an average size of crystallites (~ 0.1 - 1 μm) which in many cases are ideal for X-ray powder diffraction (XRPD). To date, a series of experiments and data analyses have been carried out, which demonstrate the validity of XRPD to study microcrystalline protein samples. This method is powerful for high-throughput polymorph identification and crystal screening and also suitable for structure solution. In this webinar, we demonstrate the complementarity of laboratory and synchrotron XRPD as an analysis tool in protein crystallography. Parametric measurements (variation of relative humidity or pH) will be presented on pharmaceutical proteins and their complexes with organic ligands. A question and answer session will conclude the presentation.
Application of microcalorimetry in drug discovery at Exelixis
See the value of ITC for SMDD . Differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC) have been extensively applied in our highly integrated small molecule drug discovery platform at Exelixis Inc. In this report, we will illustrate the utility of calorimetry in making better laboratory decisions. Examples will include improved protein construct selection for scale-up; direct measurement of the effects of mutations and post-translational modifications on protein stability; rapid optimization of solvent formulation; direct measurement of substrate and inhibitor binding affinity; determination of the mode of inhibitor binding; characterization of protein-protein interactions; and improved structural biology efficiency, when used in conjunction of other biophysical methods..
Made to measure viral drug delivery
While viruses are so often seen as the enemy, modern scientific techniques may soon be able to harness the strengths of a virus for drug delivery systems that are designed to treat diseases, rather than cause them. Using a Zetasizer Nano particle characterization system from Malvern Instruments, researchers at Indiana University’s (IU) Molecular and Cellular Biochemistry Department have been studying self-assembled virus-based drug delivery systems that can be tuned to a particular size enabling the uptake of specific functional cargo.. Dr Stella Aniagyei, post doctoral research associate at the IU’s Molecular and Cellular Biochemistry department explains: “Viruses tend to be nanosized, symmetrical and structurally consistent with a narrow size distribution. Despite this apparent biological simplicity, viruses are extremely good at delivering their own genome to living biological tissue. This makes them a prime target for biological engineers looking for an efficient transportation device that will deliver drug directly to infected cells.”. “Here at IU’s Nanocharacterization facility, the Malvern Zetasizer Nano is the ‘go to’ instrument for characterization of assembled product,” said Dr Aniagyei. “Structures closely resembling virus give a narrow size distribution. If they don’t, then we know the process has gone off the biological path. We are currently looking at aggregation limits to move towards defining optimum ionic conditions for the assembly of nucleic acid binding to Gag proteins [one of the nine genes in the retrovirus RNA genome].”. Malvern’s Zetasizer range uses light scattering techniques to measure hydrodynamic size, zeta potential and molecular weight of proteins and nanoparticles. According to Dr Aniagyei, “Malvern’s Zetasizer Nano is very useful for protein characterization. The ease with which it can be used makes it the perfect instrument for the student environment. It definitely is one of the easiest instruments I’ve had to work with.”. Indiana University (IU) is already in the spotlight having just received $900,000 from the Ovarian Cancer Research Fund, or OCRF, to help them prepare the new drug SGI-110 for clinical trials in patients whose once-thwarted ovarian cancer has returned. However, this work is not the only IU project at the cutting edge. Established on July 1 2009, the Department of Molecular and Cellular Biochemistry was the first science department created on the Indiana University Bloomington campus in 33 years. Linking biology, chemistry, and medical sciences, the department’s main focus is on the priority areas of structural virology and virus assembly.. For more details about the Zetasizer Nano go to www.malvern.com/zetasizer. For more about the work of Indiana University’s Molecular and Cellular Biochemistry department visit http://www.indiana.edu/~mcbdept. Malvern, Malvern Instruments and Zetasizer are registered trademarks of Malvern Instruments Ltd.
X-rays are scattered by the electrons in a material. From the measured interference pattern of all scattered waves one can deduce information about nanoscale and atomic order and disorder in a given sample. From periodically structured materials discrete Bragg scattering is observed, whereas diffuse scattering prevails in case of disordered materials..
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