ArticleBiophysical journal2010
A method for removing effects of nonspecific binding on the distribution of binding stoichiometries: application to mass spectroscopy data.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 30 citations in OpenAlex.
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- Structural basis of nearest-neighbor cooperativity in the ring-shaped gene regulatory protein TRAP from protein engineering and cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Fragment-based drug discovery campaigns guided by native mass spectrometry.RSC medicinal chemistry · 2024Review
- Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry.Journal of visualized experiments : JoVE · 2018Article
- Quantifying the binding stoichiometry and affinity of histo-blood group antigen oligosaccharides for human noroviruses.Glycobiology · 2018Article
- Optimization of Electrospray Ionization by Statistical Design of Experiments and Response Surface Methodology: Protein-Ligand Equilibrium Dissociation Constant Determinations.Journal of the American Society for Mass Spectrometry · 2016Article
- Native Mass Spectrometry in Fragment-Based Drug Discovery.Molecules (Basel, Switzerland) · 2016Review
- Probing allosteric mechanisms using native mass spectrometry.Current opinion in structural biology · 2015Review
- Deconvolution method for specific and nonspecific binding of ligand to multiprotein complex by native mass spectrometry.Analytical chemistry · 2015Article
- Allosteric mechanisms can be distinguished using structural mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Reliable determinations of protein-ligand interactions by direct ESI-MS measurements. Are we there yet?Journal of the American Society for Mass Spectrometry · 2012Article
- Complexes of the outer mitochondrial membrane protein mitoNEET with resveratrol-3-sulfate.Biochemistry · 2011Article
- Quantifying Protein-Glycan Interactions Using Native Mass Spectrometry.Mass spectrometry reviewsReview
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
There is often an interest in knowing, for a given ligand concentration, how many protein molecules have one, two, three, etc. ligands bound in a specific manner. This is a question that cannot be addressed using conventional ensemble techniques. Here, a mathematical method is presented for separating specific from nonspecific binding in nonensemble studies. The method provides a way to determine the distribution of specific binding stoichiometries at any ligand concentration when using nonensemble (e.g., single-molecule) methods. The applicability of the method is demonstrated for ADP binding to creatine kinase using mass spectroscopy data. A major advantage of our method, which can be applied to any protein-ligand system, is that no previous information regarding the mechanism of ligand interaction is required.
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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.