<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Willmer P</submitter><funding>Innovationsfonden</funding><pagination>19498-19504</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12444738</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>97(36)</volume><pubmed_abstract>Characterizing the kinetics of biomolecular interactions is fundamental for understanding biological mechanisms, developing novel drugs for advancing healthcare and for optimizing processes in protein engineering. Although modern surface-based methods have advanced our understanding of protein-protein and protein-ligand kinetics, they rely on immobilized samples, preventing the study of interactions under native conditions and leading to an incomplete understanding. In this work, we propose a paradigm shift by introducing a new method based on flow-induced dispersion analysis to study interaction kinetics while keeping biomolecules in solution, eliminating the need for surface immobilization and thereby preserving molecular mobility and avoiding structural constraints. The method examines </pubmed_abstract><journal>Analytical chemistry</journal><pubmed_title>In-Solution Characterization of Biomolecular Interaction Kinetics under Native Conditions.</pubmed_title><pmcid>PMC12444738</pmcid><funding_grant_id>2052-00002B</funding_grant_id><pubmed_authors>Hundahl AC</pubmed_authors><pubmed_authors>Willmer P</pubmed_authors><pubmed_authors>Marie R</pubmed_authors><pubmed_authors>Jensen H</pubmed_authors><pubmed_authors>Sahni Ray K</pubmed_authors><pubmed_authors>Stender EGP</pubmed_authors></additional><is_claimable>false</is_claimable><name>In-Solution Characterization of Biomolecular Interaction Kinetics under Native Conditions.</name><description>Characterizing the kinetics of biomolecular interactions is fundamental for understanding biological mechanisms, developing novel drugs for advancing healthcare and for optimizing processes in protein engineering. Although modern surface-based methods have advanced our understanding of protein-protein and protein-ligand kinetics, they rely on immobilized samples, preventing the study of interactions under native conditions and leading to an incomplete understanding. In this work, we propose a paradigm shift by introducing a new method based on flow-induced dispersion analysis to study interaction kinetics while keeping biomolecules in solution, eliminating the need for surface immobilization and thereby preserving molecular mobility and avoiding structural constraints. The method examines </description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Sep</publication><modification>2026-06-03T15:20:54.148Z</modification><creation>2026-04-29T03:12:56.957Z</creation></dates><accession>S-EPMC12444738</accession><cross_references><pubmed>40882972</pubmed><doi>10.1021/acs.analchem.5c02164</doi></cross_references></HashMap>