ArticleJournal of biological physics2004
Dynamic light scattering application to study protein interactions in electrolyte solutions.
Article in Journal of biological physics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 59 citations in OpenAlex.
- Article
- CLASP2 binding to curved microtubule tips promotes flux and stabilizes kinetochore attachments.The Journal of cell biology · 2020Article
- Nanoparticles without and with protein corona: van der Waals and hydration interaction.Journal of biological physics · 2019Article
- High Throughput Prediction Approach for Monoclonal Antibody Aggregation at High Concentration.Pharmaceutical research · 2017Article
- Challenges in Predicting Protein-Protein Interactions from Measurements of Molecular Diffusivity.Biophysical journal · 2016Article
- Use of dynamic light scattering and small-angle X-ray scattering to characterize new surfactants in solution conditions for membrane-protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Protein-protein interactions in dilute to concentrated solutions: α-chymotrypsinogen in acidic conditions.The journal of physical chemistry. B · 2014Article
- Effects of an anticarcinogenic Bowman-Birk protease inhibitor on purified 20S proteasome and MCF-7 breast cancer cells.PloS one · 2014Article
- Assessment and significance of protein-protein interactions during development of protein biopharmaceuticals.Biophysical reviews · 2013Review
- Establishing a link between amino acid sequences and self-associating and viscoelastic behavior of two closely related monoclonal antibodies.Pharmaceutical research · 2011Article
- Altered phase diagram due to a single point mutation in human gammaD-crystallin.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The concentration dependence of the diffusion coefficient of particles suspended in solution depends primarily on the occupied volume fraction and on repulsive and attractive forces. This dependency is expressed by the interaction parameter, which can be assessed experimentally by light scattering measurements and have been determined for the diffusion coefficient of BSA under different salt concentration conditions in the present work. The result shows that the diffusion coefficient of protein grows up with increasing protein concentration, and when the ionic strength turns up gradually the diffusion coefficient decreases with protein concentration's increasing. The concentration dependence of BSA diffusion coefficients is interpreted in the context of a two-body potential of mean force, which includes repulsive hard-sphere and Coulombic interactions and attractive dispersion. With the increase of ionic strength, Debye screening decreases, protein interaction changes from repulsion to attraction, and protein begins to aggregate. By means of the concentration dependence of BSA diffusion coefficients, one can obtain the parameters of protein interactions and can find that protein bears a net effective charge of -9.0 e and has a Hamaker constant of 2.8k(B)T. This work demonstrates that DLS is an effective technique of studying protein interactions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.