Research Topics
Genomes and GenesSpecies | A P MintonSummaryAffiliation: National Institutes of Health Country: USA Publications
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Publications
Effects of inert volume-excluding macromolecules on protein fiber formation. II. Kinetic models for nucleated fiber growthDamien Hall
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA
Biophys Chem 107:299-316. 2004..In contrast, the rate of redistribution of fiber length, which occurs on a much slower time scale than polymer formation, is found to be insensitive to the extent of crowding...- Macromolecular crowdingAllen P Minton
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892-0830, USA
Curr Biol 16:R269-71. 2006 - Macromolecular crowding stabilizes the molten globule form of apomyoglobin with respect to both cold and heat unfoldingPeter McPhie
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, NIDDK, NIH, Bethesda, MD 20892 0830, USA
J Mol Biol 361:7-10. 2006..Two-state analysis of the data shows that the effects of salt and polymer are additive, and that stabilization by the polymer is independent of temperature, as predicted by excluded volume theory... 
Effective hard particle model for the osmotic pressure of highly concentrated binary protein solutionsAllen P Minton
Biophys J 94:L57-9. 2008..The size of this sphere is determined by analysis of the concentration dependence of the osmotic pressure of the isolated protein...- Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteinsCristina Fernandez
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda Maryland, USA
Biophys J 96:1992-8. 2009.... - Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowdingAllen P Minton
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD
Biopolymers 99:239-44. 2013..2012Wiley Periodicals, Inc. Biopolymers 99: 239-244, 2013... - Hard quasispherical particle models for the viscosity of solutions of protein mixturesAllen P Minton
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, Maryland 20892 0830, USA
J Phys Chem B 116:9310-5. 2012..Soc. Rheol. 1959, 3, 137) . Further generalization of these equations to treat the concentration-dependent viscosity of self-associating proteins is suggested... - The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other nonassociating proteinsAllen P Minton
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, NIH DHHS, Bethesda, MD 20892 0830, USA
J Pharm Sci 96:3466-9. 2007..The pH dependence of the effective volume is shown to agree well with that previously obtained from analysis of the concentration dependence of sedimentation equilibrium and static light scattering... - Static light scattering from concentrated protein solutions, I: General theory for protein mixtures and application to self-associating proteinsAllen P Minton
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, Maryland, USA
Biophys J 93:1321-8. 2007..It is shown that by using these relations one can extract from the data reasonably reliable information about underlying weak associations that are manifested only at very high total protein concentration... - How can biochemical reactions within cells differ from those in test tubes?Allen P Minton
Section on Physical Biochemistry, Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health U S DHHS, Bethesda, MD 20892, USA
J Cell Sci 119:2863-9. 2006..Greater than order-of-magnitude increases in association rate and equilibrium constants attributable to background interactions have been observed in simulated and actual intracellular environments... - Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observationsAllen P Minton
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Public Health Service, Bethesda, MD, USA
J Pharm Sci 94:1668-75. 2005..Possible effects of the effect of crowding on an initially native protein that can undergo unfolding, self-association of native protein, and/or aggregation of non-native protein are considered... - Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: macromolecular crowding and protein stability revisitedAllen P Minton
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, United States Department of Health and Human Services, Bethesda, MD 20892 0830, USA
Biophys J 88:971-85. 2005..Predicted effects are in qualitative and/or semiquantitative accord with the results of several published experimental studies... - Effects of excluded surface area and adsorbate clustering on surface adsorption of proteins. II. Kinetic modelsA P Minton
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0830 USA
Biophys J 80:1641-8. 2001.... - Analysis of membrane binding equilibria of peripheral proteins: allowance for excluded area of bound proteinAllen P Minton
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
Anal Biochem 397:247-9. 2010.... - Influence of excluded volume upon macromolecular structure and associations in 'crowded' mediaA P Minton
Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, Building 8, Room 226, National Institutes of Health, Bethesda, MD 20892 0830, USA
Curr Opin Biotechnol 8:65-9. 1997..Recent theoretical studies have improved incrementally our ability to understand and model excluded volume effects in simple model systems... - Quantitative characterization of reversible macromolecular associations via sedimentation equilibrium: an introductionA P Minton
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0830, USA
Exp Mol Med 32:1-5. 2000.... - Protein folding: Thickening the brothA P Minton
Building 8, Room 226, NIH, Bethesda, 20892 0830, USA
Curr Biol 10:R97-9. 2000..The results can be rationalised in terms of kinetic competition between distinct processes, taking into account the relative influence of crowding on each process... - Effect of a concentrated "inert" macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: a statistical-thermodynamic modelA P Minton
Section on Physical Biochemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0830, USA
Biophys J 78:101-9. 2000.... - Effects of excluded surface area and adsorbate clustering on surface adsorption of proteins I. Equilibrium modelsA P Minton
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0830, USA
Biophys Chem 86:239-47. 2000.... - Adsorption of globular proteins on locally planar surfaces. II. Models for the effect of multiple adsorbate conformations on adsorption equilibria and kineticsA P Minton
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892 0830
Biophys J 76:176-87. 1999.... - Quantitative characterization of polymer-polymer, protein-protein, and polymer-protein interaction via tracer sedimentation equilibriumAdedayo A Fodeke
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, Maryland 20892, USA
J Phys Chem B 114:10876-80. 2010..The measured dependences may be accounted for quantitatively by a simple model in which BSA and Ficoll 70 are represented by equivalent rigid particles... - Self-association of Zn-insulin at neutral pH: investigation by concentration gradient--static and dynamic light scatteringArun K Attri
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
Biophys Chem 148:23-7. 2010.... - pH-dependent self-association of zinc-free insulin characterized by concentration-gradient static light scatteringArun K Attri
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U S Department of Health and Human Services, Bethesda, MD 20892, USA
Biophys Chem 148:28-33. 2010..0, and the best-fit value of the stepwise equilibrium constant obtained therefrom was in excellent agreement with that obtained from analysis of the light scattering data obtained at pH 7.2... - Macromolecular crowding: qualitative and semiquantitative successes, quantitative challengesDamien Hall
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, MD 20892-0830, USA
Biochim Biophys Acta 1649:127-39. 2003..Recently suggested novel approaches to quantitative analysis of crowding phenomena, which may help to overcome some of the limitations of current theory, are summarized... - Effects of inert volume-excluding macromolecules on protein fiber formation. I. Equilibrium modelsDamien Hall
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Biophys Chem 98:93-104. 2002..It is found that the fractional (logarithmic) change in both solubility and in the breadth of the polymer size distribution scale almost linearly with the fractional (logarithmic) change in the thermodynamic activity of monomer... - New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteinsArun K Attri
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, MD 20892, USA
Anal Biochem 337:103-10. 2005.... - Automated measurement of the static light scattering of macromolecular solutions over a broad range of concentrationsCristina Fernandez
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Building 8, Bethesda, MD 20892, USA
Anal Biochem 381:254-7. 2008..The experimentally obtained concentration dependence of scattering obtained from all three proteins is quantitatively consistent with the assumption that no significant self-association occurs over the measured range of concentrations... - Effect of high concentration of inert cosolutes on the refolding of an enzyme: carbonic anhydrase B in sucrose and ficoll 70Begoña Monterroso
Laboratory of Biochemistry and Genetics, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 282:33452-8. 2007..Acceleration of the side reaction by Ficoll is significantly greater than that of sucrose at equal w/v concentrations... - Composition gradient static light scattering: a new technique for rapid detection and quantitative characterization of reversible macromolecular hetero-associations in solutionArun K Attri
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, MD 20892, USA
Anal Biochem 346:132-8. 2005..The results of validation experiments demonstrate that the technique can correctly identify complexes and reliably evaluate equilibrium constants for hetero-association... - Effect of dextran on protein stability and conformation attributed to macromolecular crowdingKenji Sasahara
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
J Mol Biol 326:1227-37. 2003..Both observations are in qualitative accord with predictions of a previously proposed model for the effect of intermolecular excluded volume (macromolecular crowding) on protein stability and conformation... - Implications of macromolecular crowding for protein assemblyA P Minton
Laboratory of Biochemistry and Genetics, Section on Physical Biochemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 0830, USA
Curr Opin Struct Biol 10:34-9. 2000..Under certain pathological conditions, 'overcrowding' may enhance the formation of nonfunctional aggregates of non-native protein (e.g. amyloid and inclusion bodies)... - Rapid quantitative characterization of protein interactions by composition gradient static light scatteringKeiichi Kameyama
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, Maryland 20892-0830, USA
Biophys J 90:2164-9. 2006.... - Kinetic analysis of biosensor data: elementary tests for self-consistencyP Schuck
Section of Physical Biochemistry, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Trends Biochem Sci 21:458-60. 1996..A search of the recent literature reveals that many published results fail these tests qualitatively... - Cell biology: join the crowdR John Ellis
Nature 425:27-8. 2003 - Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonucleaseSilvia Zorrilla
, CSIC, Madrid, Spain
Biophys Chem 108:89-100. 2004..4, upon total protein concentration. Experimental results are interpreted in the context of a model for weak self-association leading to the formation of significant amounts of oligomers at total protein concentrations exceeding 25 g/l... - Non-ideal tracer sedimentation equilibrium: a powerful tool for the characterization of macromolecular interactions in crowded solutionsGerman Rivas
Centro de Investigaciones Biologicas, Consejo Superior de Investigaciones Cientificas, 28040 Madrid, Spain
J Mol Recognit 17:362-7. 2004..A new analysis of experimental data is presented that requires no a priori assumptions regarding the nature of weak repulsive interactions between solute species and the concentrated (crowding) species... - Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequencesHuan Xiang Zhou
Department of Physics and Institute of Molecular Biophysics and School of Computational Science, Florida State University, Tallahassee, Florida 32306, USA
Annu Rev Biophys 37:375-97. 2008..Theoretical and experimental approaches to the characterization of crowding- and confinement-induced effects in systems approaching the complexity of living organisms are suggested... - Turbidity as a probe of tubulin polymerization kinetics: a theoretical and experimental re-examinationDamien Hall
Department of Chemistry, Cambridge University, Cambridge CB2 1EW, UK
Anal Biochem 345:198-213. 2005..4). We believe that the general findings and principles outlined here are applicable to studies of other fibril-forming systems that use turbidity as a marker of polymerization progress... - Protein aggregation in crowded environmentsR John Ellis
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
Biol Chem 387:485-97. 2006..This review discusses the quantitative effects of crowding on protein aggregation and the role of molecular chaperones in combating this problem... - Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-IIDanny M Hatters
Russell Grimwade School of Biochemistry and Molecular Biology, The University of Melbourne, Victoria 3010, Australia
J Biol Chem 277:7824-30. 2002..The model predicts that an increase in the fractional volume occupancy of macromolecules in a physiological fluid can nonspecifically accelerate the formation of amyloid fibers by any amyloidogenic protein... - Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrilsJose Manuel Gonzalez
Centro de Investigaciones Biológicas and Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Cientificas, 28040 Madrid, Spain
Proc Natl Acad Sci U S A 102:1895-900. 2005..The proposed model is in accord with the results obtained from our experimental observations... - Quantitative characterization of weak self-association in concentrated solutions of immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressureMercedes Jimenez
Department of Protein Science, Centro de Investigaciones Biologicas, Consejo Superior de Investigaciones Cientificas, E 28040 Madrid, Spain
Biochemistry 46:8373-8. 2007..Both sets of data are quantitatively accounted for by a model in which IgG self-associates at very high concentration to form (predominantly) trimers under the conditions of these experiments... - A simple semiempirical model for the effect of molecular confinement upon the rate of protein foldingManajit Hayer-Hartl
Department of Cellular Biochemistry, Max Planck Institute for Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany
Biochemistry 45:13356-60. 2006.... - Analytical ultracentrifugation for the study of protein association and assemblyGeoffrey J Howlett
Department of Biochemistry and Molecular Biology and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Victoria, Australia
Curr Opin Chem Biol 10:430-6. 2006....