3 edition of Protein crystal nucleation kinetics using relative light-scattering techniques found in the catalog.
Protein crystal nucleation kinetics using relative light-scattering techniques
1989 by National Aeronautics and Space Administration, George C. Marshall Space Flight Center, For sale by the National Technical Information Service in [Marshall Space Flight Center, Ala.], [Springfield, Va .
Written in English
|Statement||by Marc Lee Pusey.|
|Series||NASA technical memorandum -- NASA TM-100348., NASA technical memorandum -- 100348.|
|Contributions||George C. Marshall Space Flight Center.|
|The Physical Object|
Purified protein quality control is the final and critical check-point of any protein production process. Unfortunately, it is too often overlooked and performed hastily, resulting in irreproducible and misleading observations in downstream applications. In this review, we aim at proposing a simple-to-follow workflow based on an ensemble of widely available physico . A colloidal crystal is an ordered array of colloid particles and fine grained materials analogous to a standard crystal whose repeating subunits are atoms or molecules. A natural example of this phenomenon can be found in the gem opal, where spheres of silica assume a close-packed locally periodic structure under moderate compression. Bulk properties of a colloidal crystal . Complementary techniques such as spectroscopy, mass-spectrometry, analytical ultracentrifugation, activity assays, static or dynamic light scattering (SLS/DLS), small angle X-ray scattering (SAXS) are very valuable methods to gain both quantitative and qualitative insights about your protein sample. Thus, the crystallization and/or nucleation techniques described herein can provide a greater ability to control the crystal phase of the pharmaceutically active agent, and/or the reduce or eliminate processing steps which may result in changes in the crystal phase that may occur during these steps (e.g., see FIG. 2).
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Get this from a library. Protein crystal nucleation kinetics using relative light-scattering techniques: Center Director's discretionary fund final report.
A combination of small angle X-ray scattering and gel techniques was used to follow the kinetics of protein crystal growth as a function of time.
Hen egg white lysozyme, at different protein. Equilibrium crystal shapes, energy barriers, and the kinetics of protein crystal nucleation are treated from the same molecular-kinetic standpoint by introducing a concept for bond selection.
visualize elementary acts during protein and virus crystal growth [59,60], while the sizes of the protein crystal nuclei are determined by means of thermodynamic estimations. Using LCM-DIM, Sazaki’s group studies the 2-D nucleation kinetics of lysozyme  and glucose isomerase crystals (under high pressure) .Cited by: 3.
A variety of different nucleation scenarios have been loosely labeled as two-step, from crystal nucleation in colloids (see section ) or Lennard-Jones liquids (see section ) to the formation of crystals of urea or NaCl (see section ), not to mention biomineralization (see, e.g., refs (18 and 53)) and Protein crystal nucleation kinetics using relative light-scattering techniques book crystallization (see, e.g Cited by: Alzheimer's, Parkinson's, and Huntington's diseases and systemic amyloidosis are pathologies wherein proteins aggregatein vivo to form insoluble deposits (1, 2).
In vitro studies have documented that many amyloidogenic proteins assemble irreversibly into fibrils via a nucleation-dependent pathway (3, 4).Protein aggregation occurs through specific. Dynamic light scattering, and small-angle X-ray, and small-angle neutron diffraction mostly inform on the interactions in supersaturated (crystallizing) solutions, but light scattering data are difficult to interpret unambiguously (Galkin and Vekilov, ).
To gain some insight into the actual nucleation mechanism direct visualization of the Cited by: The reasons for BSM and its impact on protein crystal nucleation are considered in full detail in a review paper.
Shape of the Protein Crystal Nucleus. Crystal nucleation kinetics is studied intensively with globular proteins, but the experimental determination of the shape of the crystal nucleus still remains a by: 6. The classical theory overestimates the crystal nucleation rate by 10 orders of magnitude.
To understand puzzle (iii) above, we use Eq. (3) for an estimate of the crystal nucleation rate based on the classical nucleation theory.
The rate ν* can be evaluated form the rate of attachment of molecules to lysozyme crystals at similar protein. foresee even faster nucleation in the region of L–L demixing beyond the critical point (8).
In view of the practical importance of the protein crystal nucleation and the need for a better understanding of the phase behavior of protein solutions, we set out to study experimentally the nucleation kinetics around the L–L separation boundary.
1 Introduction to protein crystallisation. General principles of crystallisation theory. The word 'crystal' is derived from the Greek word 'krustallos' (clear ice).Like ice, crystals are physically homogeneous solids; many of them have a transparent glittering appearance and a well-defined geometrical shape, with regular faces and sharp edges.
Most recently, some sophisticated techniques for protein crystallization using dc (in the range of 2–6 µA) and ac (in the range of 2–8 Hz) have enabled control over crystal nucleation, size and orientation (the latter governed by a rather strong magnetic field of T).
These techniques allow for obtaining large and suitable crystals Cited by: 3. We use static light scattering (SLS) to delineate the relative roles of Mg 2+ and Na + (see Supplementary Fig. 4 and Supplementary Note 1).The colloidal stability of Cited by: Please use one of the following formats to cite this article in your essay, paper or report: APA.
Malvern Panalytical. (, September 03). Dynamic Light Scattering as a Method for Understanding the Colloidal Stability of Protein : Malvern Panalytical. New Strategies for Protein Crystal Growth - Class Websites Published by Guset User, Description: PROTEIN CRYSTALLIZATION FIGURE 1 Some typical pro-tein crystals of lysozyme.
crystal nucleus. Close to this critical point, the free-energy barrier for crystal nucleation is strongly reduced and hence, the crystal nucleation rate increases by many orders of magnitude.
Because the location of the metastable critical point can be controlled by changing the composition of the solvent, the present work suggests a systematic ap.
Protein-dense liquid clusters are regions of high protein concentration that have been observed in solutions of several proteins. The typical cluster size varies from several tens to several hundreds of nanometres and their volume fraction remains below 10−3 of the solution.
According to the two-step mechanism of nucleation, the protein-rich clusters serve as locations for and precursors to Cited by: Light scattering offers two distinct means of assessing the quality and purity of protein samples: dynamic light scattering and size exclusion chromatography coupled to multi-angle light scattering.
DLS is an excellent means for obtaining rapid, qualitative estimates of aggregation and impurities in a protein solution, with minimal sample.
Protein Analysis by Dynamic Light Scattering: Methods and Techniques for Studentsz Light scattering measurements have numerous appli-cations in condensed matter physics [1–3], biology [4–7], remain monodisperse during crystal nucleation and growth [16–21].
In most universities, the light scattering technology is. Two site-specific mutants of a biosynthetic protein from Campylobacter jejuni were prepared in order to improve the diffraction properties of these crystals.
The initial DLS of these samples in buffer—10 mM (4-(2-hydroxyethyl) piperazineethanesulfonic acid [HEPES]), pHM NaCl—is shown in Figure 1a and order to remove protein aggregates, the samples. Light scattering is a non-invasive technique that has received wide acceptance in the area of protein and formulation characterization.
Light Scattering as a Characterization Tool The scattering intensity of a small molecule is proportional to the square of the molecular : Malvern Panalytical. Dynamic light scattering (DLS) has become an increasingly popular tool for screeing tool for crystallography since the early 's.
Its use in protein crystallisatio0n screening is described taking into account aspects such as particle size determination, aggregation and EndoPG I : Malvern Panalytical. nucleation of individual HbS fibers indicates that the process is random and follows statistics similar to those established for nucleation of crystals or liquid droplets from vapors.
Thermodynamics and interactions in aqueous solutions of proteins. We used chromatographic, static and dynamic light scattering techniques, and atomic force. Protein characterization by static light scattering Introduction to static light scattering Static light scattering (SLS) is a non-invasive technique whereby an absolute molecular mass of a protein sample in solution may be experimentally determined to an accuracy of better than 5% through exposure to low intensity laser light ( nm).
Predicting protein crystallization from a dilute solution property. Acta Crystallogr D Giege R, Ducruix A. Eds. Crystallization of Nucleic Acids and Proteins: A Practical Approach (Practical Approach Series, ) Oxford University Press, New York. Kratochvil P. Classic light scattering from polymer solutions.
Elsevier. P.R. Ten Wolde and D. Frenkel () Enhancement of protein crystal nucleation by critical density fluctuations, Scie – O. Galkin and P.G. Vekilov () Control of protein crystal nucleation around the metastable liquid-liquid phase boundary, Proc.
Natl. Acad. Sci. U.S.A. 97, – Author: C. Mahadevan. Light, oxygen, voltage (LOV) photoreceptors consist of conserved photo-responsive domains in bacteria, archaea, plants and fungi, and detect blue-light via a flavin cofactor.
We investigated the blue-light induced conformational transition of the dimeric photoreceptor PpSB1-LOV-R66I from Pseudomonas putida in solution by using small-angle X-ray scattering (SAXS).Cited by: 5. A further technique uses crystals of a similar protein (e.g., mutant protein, same protein from a different species) to promote nucleation.
In this case, we speak of by: dynamics of the scatterer, which gave rise to the acronym DLS (dynamic light scattering) . Photon correlation spectroscopy has become a powerful light-scattering technique for study-ing the properties of suspensions and solutions of colloids, biological solutions, macromolecules and polymers, that is absolute, non-invasive and Size: 1MB.
Chadwick et al., Heteroepitixial Control of Crystal Nucleation Using Crystalline Substrates. Oral presentation at the annual meeting of the American Institute of Chemical Engineers.
Oct. Nov. 2, Pittsburgh, PA. Chadwick et al., Polymorphic control by heterogeneous nucleation—A new method for selecting crystalline substrates. Please use one of the following formats to cite this article in your essay, paper or report: APA.
Malvern Panalytical. (, September 03). The Determination of Protein Structure and Stability by Combining Dynamic Light Scattering and Raman : Malvern Panalytical. Accordingly, the solution behavior of the bacterial outer membrane protein OmpF porin was studied by static light scattering under conditions favorable for crystal growth.
The second osmotic virial coefficient (B 22) was found to be a predictor of the crystallization behavior of porin, as has previously been found for soluble proteins. The combination of SEC with downstream light scattering analysis and the development of columns that can be used for ultra high-pressure liquid chromatography (UHPLC)-based SEC are overcoming many of the limitations of SEC and enabling more detailed protein characterization.
light scattering (DLS), static light scattering,14,17 fluores-cence spectroscopy,19 electrophoretic light scattering,14,15,17,19,20 circular dichroism,21 and size-exclusion chromatography,23 However, in many cases, these techniques provide indirect or less quantitative evidence about the degree of protein binding.
Thaumatin is frequently used as a model protein in crystallization studies because it rapidly forms crystals in the presence of tartrate ions.
The thermodynamic and kinetic properties of thaumatin crystals have been studied for almost 10 years, and the results are contradictory. Here we show that by using a homogeneous preparation of thaumatin and controlling the stereochemistry of Cited by: 7.
Protein Characterization by Static Light Scattering Ewa Folta-Stogniew Yale University • Light Scattering Technologies – Static and dynamic light scattering – Parameters derived from SLS and DLS measurements • Detection and differentiation between low order oligomers and highFile Size: 1MB.
Accelerate protein crystal growth by protein thin film template. Pechkova and Nicolini. Journal of Crystal Growth () Development of a technology for automation and miniaturization of protein crystallization.
Mueller et al. Journal of Biotechnology 85 () BIOPOLYMERS VOL. 12, () Electrophoretic Light Scattering as a Probe of Reaction Kinetics* B. BERNEt and RINA GINGER, Columbia University, New York, New York synopsis A new method is proposed for determining.
Differences in population based on molar mass distribution x10 4 x10 5 x10 6 x10 7 x10 8 x10 9 Cumulative Weight Fraction W Molar Mass (g/mol) Cumulative Molar Mass OVA_e_UV OVA_a_UV. This distribution was very relevant to understand rheological properties.
To improve resolution, a mix of Nile blue and Nile red dyes was dissolved in the melted samples in proportions that did not modify the nucleation kinetics. When the high melting fraction of milk fat was studied the effect of processing conditions on microstructure was Cited by: 2. Since protein function is determined by structure, high quality protein crystals must be grown in order to determine their structure by X-ray crystallography.
The book also discusses diseases that occur due to undesired protein condensation, an increasingly important subject. Examples include sickle cell anemia, cataracts and Alzheimer's disease.Most ice in nature forms because of impurities which boost the exceedingly low nucleation rate of pure supercooled water.
However, the microscopic details of ice nucleation on these substances remain largely unknown. Here, we have unraveled the molecular mechanism and the kinetics of ice formation on kaolinite, a clay mineral playing a key role in climate science.Recent theoretical and experimental studies have proposed a two-step mechanism for crystal formation in which crystal nucleation is preceded by formation of disordered molecular assemblies.
Here, we investigated whether similar intermediates might also form as crystals dissolve, effectively the reverse process.
A model system of glycine in water was studied, and Cited by: