Literature DB >> 32787211

Specific Buffer Effects on the Intermolecular Interactions among Protein Molecules at Physiological pH.

Andrea Salis1,2,3, Luca Cappai1, Cristina Carucci1,2,3, Drew F Parsons4, Maura Monduzzi1,2,3.   

Abstract

BSA and lysozyme molecular motion at pH 7.15 is buffer-specific. Adsorption of buffer ions on protein surfaces modulates the protein surface charge and thus protein-protein interactions. Interactions were estimated by means of the interaction parameter kD obtained from plots of diffusion coefficients at different protein concentrations (Dapp = D0[1 + kDCprotein]) via dynamic light scattering and nuclear magnetic resonance. The obtained results agree with recent findings confirming doubts regarding the validity of the Henderson-Hasselbalch equation, which has traditionally provided a basis for understanding pH buffers of primary importance in solution chemistry, electrochemistry, and biochemistry.

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Year:  2020        PMID: 32787211     DOI: 10.1021/acs.jpclett.0c01900

Source DB:  PubMed          Journal:  J Phys Chem Lett        ISSN: 1948-7185            Impact factor:   6.475


  2 in total

Review 1.  Consequences of variability in α-synuclein fibril structure on strain biology.

Authors:  Sara A M Holec; Samantha L Liu; Amanda L Woerman
Journal:  Acta Neuropathol       Date:  2022-02-04       Impact factor: 17.088

2.  Interaction of Aqueous Bovine Serum Albumin with Silica Aerogel Microparticles: Sorption Induced Aggregation.

Authors:  Attila Forgács; Madalina Ranga; István Fábián; József Kalmár
Journal:  Int J Mol Sci       Date:  2022-03-04       Impact factor: 5.923

  2 in total

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