<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Rider RL</submitter><funding>Welch Foundation</funding><funding>National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><pagination>3028-3036</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11622221</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>35(12)</volume><pubmed_abstract>Collision-induced unfolding (CIU) has provided new levels of understanding of the stabilities and structure(s) for gas phase protein and protein complex ions formed by electrospray ionization (ESI). Variable-temperature (vT-ESI) data provide complementary information about temperature-induced folding/unfolding (TIU) reactions of solution phase ions. Results obtained by using CIU and TIU provide complementary information about stabilities of gas phase versus solution phase ions. Such comparisons may provide the most direct experimental approach to answer a long-standing question from Fred McLafferty: "For how long, under what conditions, and to what extent, can solution structure be retained without solvent?" Answers to this question require greater understanding of the (i) structure(s), st</pubmed_abstract><journal>Journal of the American Society for Mass Spectrometry</journal><pubmed_title>Structure and Stabilities of Solution and Gas Phase Protein Complexes.</pubmed_title><pmcid>PMC11622221</pmcid><funding_grant_id>A-2162-20230405</funding_grant_id><funding_grant_id>RM1GM149374</funding_grant_id><funding_grant_id>RM1 GM149374</funding_grant_id><pubmed_authors>Rider RL</pubmed_authors><pubmed_authors>Lantz C</pubmed_authors><pubmed_authors>Fan L</pubmed_authors><pubmed_authors>Russell DH</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structure and Stabilities of Solution and Gas Phase Protein Complexes.</name><description>Collision-induced unfolding (CIU) has provided new levels of understanding of the stabilities and structure(s) for gas phase protein and protein complex ions formed by electrospray ionization (ESI). Variable-temperature (vT-ESI) data provide complementary information about temperature-induced folding/unfolding (TIU) reactions of solution phase ions. Results obtained by using CIU and TIU provide complementary information about stabilities of gas phase versus solution phase ions. Such comparisons may provide the most direct experimental approach to answer a long-standing question from Fred McLafferty: "For how long, under what conditions, and to what extent, can solution structure be retained without solvent?" Answers to this question require greater understanding of the (i) structure(s), st</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Dec</publication><modification>2025-04-21T21:56:38.396Z</modification><creation>2025-04-21T21:56:38.396Z</creation></dates><accession>S-EPMC11622221</accession><cross_references><pubmed>39569632</pubmed><doi>10.1021/jasms.4c00306</doi></cross_references></HashMap>