{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T16:17:52Z","timestamp":1773332272982,"version":"3.50.1"},"reference-count":61,"publisher":"MDPI AG","issue":"14","license":[{"start":{"date-parts":[[2023,7,15]],"date-time":"2023-07-15T00:00:00Z","timestamp":1689379200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Jiangsu Natural Science Foundation for Distinguished Young Scholars","award":["BK20220084"],"award-info":[{"award-number":["BK20220084"]}]},{"name":"Jiangsu Natural Science Foundation for Distinguished Young Scholars","award":["XUEKEN2022002"],"award-info":[{"award-number":["XUEKEN2022002"]}]},{"name":"Fundamental Research Funds for the Central Universities","award":["BK20220084"],"award-info":[{"award-number":["BK20220084"]}]},{"name":"Fundamental Research Funds for the Central Universities","award":["XUEKEN2022002"],"award-info":[{"award-number":["XUEKEN2022002"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>SnRK2.6 (SUCROSE NONFERMENTING 1-RELATED PROTEIN KINASE2.6) has been characterized as a molecular switch for the intracellular abscisic acid (ABA) signal-transduction pathway. Normally, SnRK2.6 is kept in an \u201coff\u201d state, forming a binary complex with protein phosphatase type 2Cs (PP2Cs). Upon stressful conditions, SnRK2.6 turns into an \u201con\u201d state by its release from PP2Cs and then phosphorylation at Ser175. However, how the \u201don\u201d and \u201coff\u201d states for SnRK2.6 are fine-tuned, thereby controlling the initiation and braking processes of ABA signaling, is still largely unclear. SnRK2.6 activity was tightly regulated through protein post-translational modifications (PTM), such as persulfidation and phosphorylation. Taking advantage of molecular dynamics simulations, our results showed that Cys131\/137 persulfidation on SnRK2.6 induces destabilized binding and weakened interactions between SnRK2.6 and HAB1 (HYPERSENSITIVE TO ABA1), an important PP2C family protein. This unfavorable effect on the association of the SnRK2.6\u2013HAB1 complex suggests that persulfidation functions are a positive regulator of ABA signaling initiation. In addition, Ser267 phosphorylation in persulfidated SnRK2.6 renders a stable physical association between SnRK2.6 and HAB1, a key characterization for SnRK2.6 inhibition. Rather than Ser175, HAB1 cannot dephosphorylate Ser267 in SnRK2.6, which implies that the retained phosphorylation status of Ser267 could ensure that the activated SnRK2.6 reforms the binary complex to cease ABA signaling. Taken together, our findings expand current knowledge concerning the regulation of persulfidation and phosphorylation on the state transition of SnRK2.6 and provide insights into the fine-tuned mechanism of ABA signaling.<\/jats:p>","DOI":"10.3390\/ijms241411512","type":"journal-article","created":{"date-parts":[[2023,7,17]],"date-time":"2023-07-17T00:35:04Z","timestamp":1689554104000},"page":"11512","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["The Modulation of Sucrose Nonfermenting 1-Related Protein Kinase 2.6 State by Persulfidation and Phosphorylation: Insights from Molecular Dynamics Simulations"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7400-7377","authenticated-orcid":false,"given":"Miaomiao","family":"Li","sequence":"first","affiliation":[{"name":"College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ting","family":"Wu","sequence":"additional","affiliation":[{"name":"College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shuhan","family":"Wang","sequence":"additional","affiliation":[{"name":"College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tianqi","family":"Duan","sequence":"additional","affiliation":[{"name":"College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Siqi","family":"Huang","sequence":"additional","affiliation":[{"name":"Institute of Bast Fiber Crops (IBFC), Chinese Academy of Agricultural Sciences (CAAS), Changsha 410205, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3503-1267","authenticated-orcid":false,"given":"Yanjie","family":"Xie","sequence":"additional","affiliation":[{"name":"College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China"},{"name":"Institute of Bast Fiber Crops (IBFC), Chinese Academy of Agricultural Sciences (CAAS), Changsha 410205, China"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2023,7,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1038\/nsmb.1842","article-title":"Post-translational modifications in signal integration","volume":"17","author":"Deribe","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Huang, J., and Xie, Y. (2023). Hydrogen Sulfide Signaling in Plants. Antioxid. Redox Signal.","DOI":"10.1089\/ars.2023.0267"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"ra72","DOI":"10.1126\/scisignal.2000464","article-title":"H2S signals through protein S-sulfhydration","volume":"2","author":"Mustafa","year":"2009","journal-title":"Sci. Signal."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"e1500968","DOI":"10.1126\/sciadv.1500968","article-title":"A novel persulfide detection method reveals protein persulfide- and polysulfide-reducing functions of thioredoxin and glutathione systems","volume":"2","author":"Pader","year":"2016","journal-title":"Sci. Adv."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"12016","DOI":"10.1021\/ja3009693","article-title":"Chemical characterization of the smallest S-nitrosothiol, HSNO; cellular cross-talk of H2S and S-nitrosothiols","volume":"134","author":"Filipovic","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"26866","DOI":"10.1074\/jbc.M115.672816","article-title":"Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide","volume":"290","author":"Cuevasanta","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1104\/pp.15.00009","article-title":"S-sulfhydration: A cysteine posttranslational modification in plant systems","volume":"168","author":"Aroca","year":"2015","journal-title":"Plant Physiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1104\/pp.18.00838","article-title":"Hydrogen Sulfide Disturbs Actin Polymerization via S-Sulfhydration Resulting in Stunted Root Hair Growth","volume":"178","author":"Li","year":"2018","journal-title":"Plant Physiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.plaphy.2020.09.020","article-title":"Hydrogen sulfide regulates the activity of antioxidant enzymes through persulfidation and improves the resistance of tomato seedling to Copper Oxide nanoparticles (CuO NPs)-induced oxidative stress","volume":"156","author":"Li","year":"2020","journal-title":"Plant Physiol. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"635470","DOI":"10.3389\/fmolb.2021.635470","article-title":"H2S Persulfidated and Increased Kinase Activity of MPK4 to Response Cold Stress in Arabidopsis","volume":"8","author":"Du","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1038\/s41438-020-00453-3","article-title":"Hydrogen sulfide promotes flowering in heading Chinese cabbage by S-sulfhydration of BraFLCs","volume":"8","author":"Ma","year":"2021","journal-title":"Hortic. Res."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.3389\/fpls.2018.01369","article-title":"Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation","volume":"9","author":"Aroca","year":"2018","journal-title":"Front. Plant Sci."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1093\/pcp\/pcx056","article-title":"Hydrogen Sulfide Regulates the Cytosolic\/Nuclear Partitioning of Glyceraldehyde-3-Phosphate Dehydrogenase by Enhancing its Nuclear Localization","volume":"58","author":"Aroca","year":"2017","journal-title":"Plant Cell Physiol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3902","DOI":"10.1105\/tpc.20.00766","article-title":"Abscisic Acid-Triggered Persulfidation of the Cys Protease ATG4 Mediates Regulation of Autophagy by Sulfide","volume":"32","author":"Aroca","year":"2020","journal-title":"Plant Cell"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"e2023604118","DOI":"10.1073\/pnas.2023604118","article-title":"Persulfidation of ATG18a regulates autophagy under ER stress in Arabidopsis","volume":"118","author":"Aroca","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/j.molp.2021.03.007","article-title":"Hydrogen sulfide-linked persulfidation of ABI4 controls ABA responses through the transactivation of MAPKKK18 in Arabidopsis","volume":"14","author":"Zhou","year":"2021","journal-title":"Mol. Plant"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1105\/tpc.19.00826","article-title":"Persulfidation-based Modification of Cysteine Desulfhydrase and the NADPH Oxidase RBOHD Controls Guard Cell Abscisic Acid Signaling","volume":"32","author":"Shen","year":"2020","journal-title":"Plant Cell"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1027730","DOI":"10.3389\/fpls.2022.1027730","article-title":"Redox post-translational modifications and their interplay in plant abiotic stress tolerance","volume":"13","author":"Almagro","year":"2022","journal-title":"Front. Plant Sci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"3340","DOI":"10.1016\/j.celrep.2018.05.044","article-title":"Arabidopsis Duodecuple Mutant of PYL ABA Receptors Reveals PYL Repression of ABA-Independent SnRK2 Activity","volume":"23","author":"Zhao","year":"2018","journal-title":"Cell Rep."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"967404","DOI":"10.3389\/fchem.2022.967404","article-title":"A briefly overview of the research progress for the abscisic acid analogues","volume":"10","author":"Liu","year":"2022","journal-title":"Front. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"4891","DOI":"10.1242\/jcs.00175","article-title":"Genome-wide gene expression profiling in Arabidopsis thaliana reveals new targets of abscisic acid and largely impaired gene regulation in the abi1-1 mutant","volume":"115","author":"Hoth","year":"2002","journal-title":"J. Cell Sci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1007\/s10142-002-0070-6","article-title":"Monitoring the expression pattern of around 7,000 Arabidopsis genes under ABA treatments using a full-length cDNA microarray","volume":"2","author":"Seki","year":"2002","journal-title":"Funct. Integr. Genom."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.cell.2006.05.050","article-title":"Different plant hormones regulate similar processes through largely nonoverlapping transcriptional responses","volume":"126","author":"Nemhauser","year":"2006","journal-title":"Cell"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1016\/j.molp.2020.01.004","article-title":"Hydrogen Sulfide Positively Regulates Abscisic Acid Signaling through Persulfidation of SnRK2.6 in Guard Cells","volume":"13","author":"Chen","year":"2020","journal-title":"Mol. Plant"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1111\/j.1744-7909.2011.01044.x","article-title":"Abscisic acid receptors: Past, present and future","volume":"53","author":"Guo","year":"2011","journal-title":"J. Integr. Plant Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1126\/science.1172408","article-title":"Regulators of PP2C phosphatase activity function as abscisic acid sensors","volume":"324","author":"Ma","year":"2009","journal-title":"Science"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1042\/BJ20091221","article-title":"Threonine at position 306 of the KAT1 potassium channel is essential for channel activity and is a target site for ABA-activated SnRK2\/OST1\/SnRK2.6 protein kinase","volume":"424","author":"Sato","year":"2009","journal-title":"Biochem. J."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1016\/j.molp.2017.07.004","article-title":"Structure of Ligand-Bound Intermediates of Crop ABA Receptors Highlights PP2C as Necessary ABA Co-receptor","volume":"10","author":"Yunta","year":"2017","journal-title":"Mol. Plant"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1074\/jbc.M111.313106","article-title":"Molecular mechanism for inhibition of a critical component in the Arabidopsis thaliana abscisic acid signal transduction pathways, SnRK2.6, by protein phosphatase ABI1","volume":"287","author":"Xie","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"4915","DOI":"10.1093\/jxb\/erx294","article-title":"Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis","volume":"68","author":"Aroca","year":"2017","journal-title":"J. Exp. Bot."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1016\/j.molp.2021.07.002","article-title":"Persulfidation-induced structural change in SnRK2.6 establishes intramolecular interaction between phosphorylation and persulfidation","volume":"14","author":"Chen","year":"2021","journal-title":"Mol. Plant"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1023\/A:1006012218704","article-title":"Molecular cloning in Arabidopsis thaliana of a new protein phosphatase 2C (PP2C) with homology to ABI1 and ABI2","volume":"38","author":"Rodriguez","year":"1998","journal-title":"Plant Mol. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"3170","DOI":"10.1105\/tpc.109.069179","article-title":"Protein phosphatases 2C regulate the activation of the Snf1-related kinase OST1 by abscisic acid in Arabidopsis","volume":"21","author":"Vlad","year":"2009","journal-title":"Plant Cell"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"17588","DOI":"10.1073\/pnas.0907095106","article-title":"Type 2C protein phosphatases directly regulate abscisic acid-activated protein kinases in Arabidopsis","volume":"106","author":"Umezawa","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1126\/science.1215106","article-title":"Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases","volume":"335","author":"Soon","year":"2012","journal-title":"Science"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"581","DOI":"10.4161\/psb.19694","article-title":"Catalytic mechanism and kinase interactions of ABA-signaling PP2C phosphatases","volume":"7","author":"Zhou","year":"2012","journal-title":"Plant Signal. Behav."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1002\/pro.2230","article-title":"Protein-protein interactions: General trends in the relationship between binding affinity and interfacial buried surface area","volume":"22","author":"Chen","year":"2013","journal-title":"Protein Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1002\/jcc.21303","article-title":"Crystal contacts as nature\u2032s docking solutions","volume":"31","author":"Krissinel","year":"2010","journal-title":"J. Comput. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"9459","DOI":"10.1073\/pnas.96.17.9459","article-title":"Cation-pi interactions in structural biology","volume":"96","author":"Gallivan","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.bpc.2006.03.001","article-title":"The improvement of the algorithm for order parameter calculation (S2) from molecular dynamics simulation using the correlation motion function","volume":"123","author":"Dubyna","year":"2006","journal-title":"Biophys. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"21259","DOI":"10.1073\/pnas.1118651109","article-title":"Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases","volume":"108","author":"Ng","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"6696","DOI":"10.1074\/jbc.R115.695056","article-title":"Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications","volume":"291","author":"Bah","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1007\/s00412-016-0591-8","article-title":"Post-translational modifications of the intrinsically disordered terminal domains of histone H1: Effects on secondary structure and chromatin dynamics","volume":"126","author":"Roque","year":"2017","journal-title":"Chromosoma."},{"key":"ref_45","first-page":"19.12.11","article-title":"Tools and procedures for visualization of proteins and other biomolecules","volume":"110","author":"Pan","year":"2015","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s10822-013-9644-8","article-title":"Protein and ligand preparation: Parameters, protocols, and influence on virtual screening enrichments","volume":"27","author":"Sastry","year":"2013","journal-title":"J. Comput. Aided Mol. Des."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1021\/acs.jctc.5b00255","article-title":"ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB","volume":"11","author":"Maier","year":"2015","journal-title":"J. Chem. Theory Comput."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1002\/jcc.10262","article-title":"Development of polyphosphate parameters for use with the AMBER force field","volume":"24","author":"Meagher","year":"2003","journal-title":"J. Comput. Chem."},{"key":"ref_49","unstructured":"Frisch, M., Trucks, G., Schlegel, H., Scuseria, G., Robb, M., Cheeseman, J., Scalmani, G., Barone, V., Mennucci, B., and Petersson, G. (2013). Gaussian 09 (Revision D.01), Gaussian, Inc."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1002\/jcc.22885","article-title":"Multiwfn: A multifunctional wavefunction analyzer","volume":"33","author":"Lu","year":"2012","journal-title":"J. Comput. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmgm.2005.12.005","article-title":"Automatic atom type and bond type perception in molecular mechanical calculations","volume":"25","author":"Wang","year":"2006","journal-title":"J. Mol. Graph. Model."},{"key":"ref_52","unstructured":"Lu, T. (2022, November 23). Sobtop, Version [Version 1.0 (dev3.1)]. Available online: https:\/\/sobereva.com\/soft\/Sobtop."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1021\/ct400751u","article-title":"Taking into Account the Ion-induced Dipole Interaction in the Nonbonded Model of Ions","volume":"10","author":"Li","year":"2014","journal-title":"J. Chem. Theory Comput."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"15460","DOI":"10.1021\/acs.jpcb.5b10423","article-title":"Force Field for Mg2+, Mn2+, Zn2+, and Cd2+ Ions That Have Balanced Interactions with Nucleic Acids","volume":"119","author":"Panteva","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1002\/jcc.20290","article-title":"The Amber biomolecular simulation programs","volume":"26","author":"Case","year":"2005","journal-title":"J. Comput. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2371","DOI":"10.1021\/ct900275y","article-title":"An Implementation of the Smooth Particle Mesh Ewald Method on GPU Hardware","volume":"5","author":"Harvey","year":"2009","journal-title":"J. Chem. Theory Comput."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0021-9991(77)90098-5","article-title":"Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes","volume":"23","author":"Ryckaert","year":"1977","journal-title":"J. Comput. Phys."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1023\/A:1009745219419","article-title":"Density-Based Clustering in Spatial Databases: The Algorithm GDBSCAN and Its Applications","volume":"2","author":"Sander","year":"1998","journal-title":"Data Min. Knowl. Discov."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"4522","DOI":"10.1021\/ja012750u","article-title":"General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation","volume":"124","author":"Prompers","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"3084","DOI":"10.1021\/ct400341p","article-title":"PTRAJ and CPPTRAJ: Software for Processing and Analysis of Molecular Dynamics Trajectory Data","volume":"9","author":"Roe","year":"2013","journal-title":"J. Chem. Theory Comput."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1002\/prot.22339","article-title":"A method for the analysis of domain movements in large biomolecular complexes","volume":"76","author":"Poornam","year":"2009","journal-title":"Proteins"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/14\/11512\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T20:12:44Z","timestamp":1760127164000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/14\/11512"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,7,15]]},"references-count":61,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2023,7]]}},"alternative-id":["ijms241411512"],"URL":"https:\/\/doi.org\/10.3390\/ijms241411512","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,7,15]]}}}