Direct fitting of sedimentation velocity data with numerical solutions of the Lamm equations has been exploited to obtain sedimentation coefficients for single solutes under conditions where solvent and solution plateaus are either not available or are transient. The calculated evolution was initialized with the first experimental scan and nonlinear regression was employed to obtain best-fit values for the sedimentation and diffusion coefficients. General properties of the Lamm equations as data analysis tools were examined. This method was applied to study a set of small peptides containing amphipathic heptad repeats with the general structure Ac-YS-(AKEAAKE)nGAR-NH2, n = 2, 3, or 4. Sedimentation velocity analysis indicated single sedimenting species with sedimentation coefficients (s(20,w) values) of 0.37, 0.45, and 0.52 S, respectively, in good agreement with sedimentation coefficients predicted by hydrodynamic theory. The described approach can be applied to synthetic boundary and conventional loading experiments, and can be extended to analyze sedimentation data for both large and small macromolecules in order to define shape, heterogeneity, and state of association.
Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate
Sedimentation of generalized systems of interacting particles. I. Solution of systems of complete Lamm equations
Sedimentation of generalized systems of interacting particles. II. Active enzyme centrifugation--theory and extensions of its validity range
Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
Nature of the difference in apparent molecular weights between the alpha subunit of urinary human chorionic gonadotropin and the alpha protein secreted by HeLa cells
Solution structure of a polypeptide containing four heptad repeat units from a merozoite surface antigen of Plasmodium falciparum
Construction of hydrodynamic bead models from high-resolution X-ray crystallographic or nuclear magnetic resonance data
Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles
SOLPRO: theory and computer program for the prediction of SOLution PROperties of rigid macromolecules and bioparticles
A two-dimensional spectrum analysis for sedimentation velocity experiments of mixtures with heterogeneity in molecular weight and shape.
A model for sedimentation in inhomogeneous media. I. Dynamic density gradients from sedimenting co-solutes
A model for sedimentation in inhomogeneous media. II. Compressibility of aqueous and organic solvents
On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
Analysis of a temperature-sensitive mutant rotavirus indicates that NSP2 octamers are the functional form of the protein
DNA recognition for virus assembly through multiple sequence-independent interactions with a helix-turn-helix motif
A new adaptive grid-size algorithm for the simulation of sedimentation velocity profiles in analytical ultracentrifugation
Evaluation of diffusion coefficients by means of an approximate steady-state condition in sedimentation velocity distributions
Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques
An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes
Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation
Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems
Slowing down single-molecule trafficking through a protein nanopore reveals intermediates for peptide translocation
Modeling analytical ultracentrifugation experiments with an adaptive space-time finite element solution of the Lamm equation
Effect of cross-linking of interfacial sodium caseinate by natural processing on the oxidative stability of oil-in-water (o/w) emulsions
Allowance for radial dilution in evaluating the concentration dependence of sedimentation coefficients for globular proteins
Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation
Brownian dynamics simulations of analytical ultracentrifugation experiments exhibiting hydrodynamic and thermodynamic non-ideality
Allowance for boundary sharpening in the determination of diffusion coefficients by sedimentation velocity: a historical perspective
Accounting for solvent signal offsets in the analysis of interferometric sedimentation velocity data.
Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes
Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation
AUC measurements of diffusion coefficients of monoclonal antibodies in the presence of human serum proteins
Measurement of length distribution of beta-lactoglobulin fibrils by multiwavelength analytical ultracentrifugation.
Novel insights into transketolase activation by cofactor binding identifies two native species subpopulations
Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease
Cajal Bodies & Gems
Cajal bodies or coiled bodies are dense foci of coilin protein. Gemini of Cajal bodies, or gems, are microscopically similar to Cajal bodies. It is believed that Cajal bodies play important roles in RNA processing while gems assist the Cajal bodies. Find the latest research on Cajal bodies and gems here.