000626436 001__ 626436
000626436 005__ 20250723105852.0
000626436 0247_ $$2doi$$a10.1042/BCJ20253036
000626436 0247_ $$2ISSN$$a1470-8728
000626436 0247_ $$2ISSN$$a0264-6021
000626436 0247_ $$2datacite_doi$$a10.3204/PUBDB-2025-01415
000626436 0247_ $$2pmid$$a40192062
000626436 0247_ $$2WOS$$aWOS:001489807200002
000626436 0247_ $$2altmetric$$aaltmetric:177417430
000626436 0247_ $$2openalex$$aopenalex:W4409212161
000626436 037__ $$aPUBDB-2025-01415
000626436 041__ $$aEnglish
000626436 082__ $$a540
000626436 1001_ $$aVarga, Soma$$b0
000626436 245__ $$aDynamic Interchange of Local Residue-Residue Interactions in the Largely Extended Single Alpha-Helix in Drebrin
000626436 260__ $$aLondon$$bPortland Press$$c2025
000626436 3367_ $$2DRIVER$$aarticle
000626436 3367_ $$2DataCite$$aOutput Types/Journal article
000626436 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1746004059_2796705
000626436 3367_ $$2BibTeX$$aARTICLE
000626436 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000626436 3367_ $$00$$2EndNote$$aJournal Article
000626436 500__ $$aISSN 1470-8728 not unique: **2 hits**.
000626436 520__ $$aSingle alpha-helices (SAHs) are protein regions with unique mechanical properties, forming long stable monomeric helical structures in solution. To date, only a few naturally occurring SAH regions have been extensively characterized, primarily from myosins, leaving the structural and dynamic variability of SAH regions largely unexplored. Drebrin (developmentally regulated brain protein) contains a predicted SAH segment with unique sequence characteristics, including aromatic residues within the SAH region and a preference for arginine over lysine in its C-terminal half. Using and NMR spectroscopy, combined with SAXS measurements, we demonstrate that the Drebrin-SAH is helical and monomeric in solution. NMR resonance assignment required specific 4D techniques to resolve severe signal overlap resulting from the low complexity and largely helical conformation of the sequence. To further characterize its structure, we generated a structural ensemble consistent with Cα, Cβ chemical shifts and SAXS data, revealing a primarily extended structure with non-uniform helicity. Our results suggest that dynamic rearrangement of salt bridges and potential transient cation-π interactions contribute to the formation and stabilization of both helical and non-helical local conformational states.
000626436 536__ $$0G:(DE-HGF)POF4-6G3$$a6G3 - PETRA III (DESY) (POF4-6G3)$$cPOF4-6G3$$fPOF IV$$x0
000626436 588__ $$aDataset connected to CrossRef, Journals: bib-pubdb1.desy.de
000626436 693__ $$0EXP:(DE-H253)P-P12-20150101$$1EXP:(DE-H253)PETRAIII-20150101$$6EXP:(DE-H253)P-P12-20150101$$aPETRA III$$fPETRA Beamline P12$$x0
000626436 7001_ $$aPéterfia, Bálint Ferenc$$b1
000626436 7001_ $$aDudola, Dániel$$b2
000626436 7001_ $$aFarkas, Viktor$$b3
000626436 7001_ $$aJeffries, Cy M.$$b4
000626436 7001_ $$aPermi, Perttu$$b5
000626436 7001_ $$00000-0002-8692-740X$$aGáspári, Zoltán$$b6$$eCorresponding author
000626436 773__ $$0PERI:(DE-600)1473095-9$$a10.1042/BCJ20253036$$gp. BCJ20253036$$n08$$p383 - 399$$tBiochemical journal$$v482$$x0006-2936$$y2025
000626436 8564_ $$uhttps://portlandpress.com/biochemj/article/doi/10.1042/BCJ20253036/235927
000626436 8564_ $$uhttps://bib-pubdb1.desy.de/record/626436/files/bcj-2025-3036.pdf$$yOpenAccess
000626436 8564_ $$uhttps://bib-pubdb1.desy.de/record/626436/files/bcj-2025-3036.pdf?subformat=pdfa$$xpdfa$$yOpenAccess
000626436 909CO $$ooai:bib-pubdb1.desy.de:626436$$pdnbdelivery$$pdriver$$pVDB$$popen_access$$popenaire
000626436 9131_ $$0G:(DE-HGF)POF4-6G3$$1G:(DE-HGF)POF4-6G0$$2G:(DE-HGF)POF4-600$$3G:(DE-HGF)POF4$$4G:(DE-HGF)POF$$aDE-HGF$$bForschungsbereich Materie$$lGroßgeräte: Materie$$vPETRA III (DESY)$$x0
000626436 9141_ $$y2025
000626436 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)0160$$2StatID$$aDBCoverage$$bEssential Science Indicators$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)1190$$2StatID$$aDBCoverage$$bBiological Abstracts$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000626436 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bBIOCHEM J : 2022$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)0113$$2StatID$$aWoS$$bScience Citation Index Expanded$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)0400$$2StatID$$aAllianz-Lizenz / DFG$$d2024-12-10$$wger
000626436 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC$$d2024-12-10
000626436 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline$$d2024-12-10
000626436 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
000626436 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bClarivate Analytics Master Journal List$$d2024-12-10
000626436 9201_ $$0I:(DE-H253)EMBL-User-20120814$$kEMBL-User$$lEMBL-User$$x0
000626436 9201_ $$0I:(DE-H253)EMBL-20120731$$kEMBL$$lEMBL$$x1
000626436 980__ $$ajournal
000626436 980__ $$aVDB
000626436 980__ $$aUNRESTRICTED
000626436 980__ $$aI:(DE-H253)EMBL-User-20120814
000626436 980__ $$aI:(DE-H253)EMBL-20120731
000626436 9801_ $$aFullTexts