{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T11:25:59Z","timestamp":1772191559439,"version":"3.50.1"},"publisher-location":"New York, NY","reference-count":76,"publisher":"Springer US","isbn-type":[{"value":"9781071620465","type":"print"},{"value":"9781071620472","type":"electronic"}],"license":[{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2022,1,1]],"date-time":"2022-01-01T00:00:00Z","timestamp":1640995200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2022]]},"DOI":"10.1007\/978-1-0716-2047-2_16","type":"book-chapter","created":{"date-parts":[[2022,2,28]],"date-time":"2022-02-28T07:02:53Z","timestamp":1646031773000},"page":"241-274","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["PELDOR Measurements on Nitroxide-Labeled Oligonucleotides"],"prefix":"10.1007","author":[{"given":"Tobias","family":"Hett","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Olav","family":"Schiemann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2022,2,28]]},"reference":[{"key":"16_CR1","volume-title":"EPR spectroscopy: fundamentals and methods. eMagRes books","year":"2018","unstructured":"Goldfarb D, Stoll S (eds) (2018) EPR spectroscopy: fundamentals and methods. eMagRes books. Wiley, Chichester, West Sussex"},{"key":"16_CR2","doi-asserted-by":"crossref","DOI":"10.1093\/oso\/9780198506348.001.0001","volume-title":"Principles of pulse electron paramagnetic resonance","author":"A Schweiger","year":"2001","unstructured":"Schweiger A, Jeschke G (2001) Principles of pulse electron paramagnetic resonance. Oxford University Press, Oxford"},{"key":"16_CR3","volume-title":"Structure and bonding","author":"CR Timmel","year":"2013","unstructured":"Timmel CR, Harmer JR (2013) Structural information from spin-labels and intrinsic paramagnetic centres in the biosciences. In: Structure and bonding, vol 152. Springer, Berlin"},{"key":"16_CR4","volume-title":"Spin-label electron paramagnetic resonance spectroscopy","author":"D Marsh","year":"2020","unstructured":"Marsh D (2020) Spin-label electron paramagnetic resonance spectroscopy. CRC Press, Taylor & Francis Group, Boca Raton"},{"issue":"24","key":"16_CR5","doi-asserted-by":"publisher","first-page":"9767","DOI":"10.1002\/anie.202004452","volume":"59","author":"N Fleck","year":"2020","unstructured":"Fleck N, Heubach CA, Hett T et al (2020) SLIM: a short-linked, highly redox-stable trityl label for high-sensitivity in-cell EPR distance measurements. Angew Chem Int Ed Engl 59(24):9767\u20139772. https:\/\/doi.org\/10.1002\/anie.202004452","journal-title":"Angew Chem Int Ed Engl"},{"issue":"15","key":"16_CR6","doi-asserted-by":"publisher","first-page":"2735","DOI":"10.3390\/molecules24152735","volume":"24","author":"JJ Jassoy","year":"2019","unstructured":"Jassoy JJ, Heubach CA, Hett T et al (2019) Site selective and efficient spin labeling of proteins with a maleimide-functionalized trityl radical for pulsed dipolar EPR spectroscopy. Molecules 24(15):2735. https:\/\/doi.org\/10.3390\/molecules24152735","journal-title":"Molecules"},{"issue":"3","key":"16_CR7","doi-asserted-by":"publisher","first-page":"1141","DOI":"10.1021\/acs.jpclett.9b03208","volume":"11","author":"Y Yang","year":"2020","unstructured":"Yang Y, Pan B-B, Tan X et al (2020) In-cell trityl-trityl distance measurements on proteins. J Phys Chem Lett 11(3):1141\u20131147. https:\/\/doi.org\/10.1021\/acs.jpclett.9b03208","journal-title":"J Phys Chem Lett"},{"key":"16_CR8","doi-asserted-by":"publisher","unstructured":"Fleck N, Heubach C, Hett T, Spicher S, Grimme S, Schiemann O (2021) Ox\u2010SLIM: synthesis of and site\u2010specific labelling with ahighly hydrophilic trityl spin label. Chem Eur J 27(16):5292-5297. https:\/\/doi.org\/10.1002\/chem.202100013","DOI":"10.1002\/chem.202100013"},{"issue":"43","key":"16_CR9","doi-asserted-by":"publisher","first-page":"15366","DOI":"10.1021\/ja508274d","volume":"136","author":"M Qi","year":"2014","unstructured":"Qi M, Gross A, Jeschke G et al (2014) Gd(III)-PyMTA label is suitable for in-cell EPR. J Am Chem Soc 136(43):15366\u201315378. https:\/\/doi.org\/10.1021\/ja508274d","journal-title":"J Am Chem Soc"},{"issue":"20","key":"16_CR10","doi-asserted-by":"publisher","first-page":"6119","DOI":"10.1021\/acs.jpclett.8b02663","volume":"9","author":"Y Yang","year":"2018","unstructured":"Yang Y, Yang F, Gong Y-J et al (2018) High sensitivity in-cell EPR distance measurements on proteins using an optimized Gd(III) spin label. J Phys Chem Lett 9(20):6119\u20136123. https:\/\/doi.org\/10.1021\/acs.jpclett.8b02663","journal-title":"J Phys Chem Lett"},{"issue":"51","key":"16_CR11","doi-asserted-by":"publisher","first-page":"23040","DOI":"10.1002\/anie.202009982","volume":"59","author":"K Singewald","year":"2020","unstructured":"Singewald K, Bogetti X, Sinha K et al (2020) Double histidine based EPR measurements at physiological temperatures permit site-specific elucidation of hidden dynamics in enzymes. Angew Chem Int Ed Engl 59(51):23040\u201323044. https:\/\/doi.org\/10.1002\/anie.202009982","journal-title":"Angew Chem Int Ed Engl"},{"issue":"21","key":"16_CR12","doi-asserted-by":"publisher","first-page":"6330","DOI":"10.1002\/anie.201501968","volume":"54","author":"TF Cunningham","year":"2015","unstructured":"Cunningham TF, Putterman MR, Desai A et al (2015) The double-histidine Cu2+-binding motif: a highly rigid, site-specific spin probe for electron spin resonance distance measurements. Angew Chem Int Ed Engl 54(21):6330\u20136334. https:\/\/doi.org\/10.1002\/anie.201501968","journal-title":"Angew Chem Int Ed Engl"},{"issue":"35","key":"16_CR13","doi-asserted-by":"publisher","first-page":"5967","DOI":"10.1021\/bi400834a","volume":"52","author":"ID Sahu","year":"2013","unstructured":"Sahu ID, McCarrick RM, Lorigan GA (2013) Use of electron paramagnetic resonance to solve biochemical problems. Biochemistry 52(35):5967\u20135984. https:\/\/doi.org\/10.1021\/bi400834a","journal-title":"Biochemistry"},{"key":"16_CR14","first-page":"975","volume":"23","author":"AD Milov","year":"1981","unstructured":"Milov AD, Salikhov KM, Schirov MD (1981) Application of ELDOR in electron-spin echo for paramagnetic center space distribution in solids. Fiz Tverd Tela 23:975\u2013982","journal-title":"Fiz Tverd Tela"},{"issue":"2","key":"16_CR15","doi-asserted-by":"publisher","first-page":"331","DOI":"10.1006\/jmre.1999.1944","volume":"142","author":"M Pannier","year":"2000","unstructured":"Pannier M, Veit S, Godt A et al (2000) Dead-time free measurement of dipole-dipole interactions between electron spins. J Magn Reson 142(2):331\u2013340. https:\/\/doi.org\/10.1006\/jmre.1999.1944","journal-title":"J Magn Reson"},{"key":"16_CR16","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1146\/annurev-physchem-032511-143716","volume":"63","author":"G Jeschke","year":"2012","unstructured":"Jeschke G (2012) DEER distance measurements on proteins. Annu Rev Phys Chem 63:419\u2013446. https:\/\/doi.org\/10.1146\/annurev-physchem-032511-143716","journal-title":"Annu Rev Phys Chem"},{"issue":"51","key":"16_CR17","doi-asserted-by":"publisher","first-page":"15905","DOI":"10.1002\/anie.201609617","volume":"55","author":"T Schmidt","year":"2016","unstructured":"Schmidt T, W\u00e4lti MA, Baber JL et al (2016) Long distance measurements up to 160 \u00c5 in the GroEL Tetradecamer using Q-band DEER EPR spectroscopy. Angew Chem Int Ed Engl 55(51):15905\u201315909. https:\/\/doi.org\/10.1002\/anie.201609617","journal-title":"Angew Chem Int Ed Engl"},{"issue":"1","key":"16_CR18","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1017\/S003358350700460X","volume":"40","author":"O Schiemann","year":"2007","unstructured":"Schiemann O, Prisner TF (2007) Long-range distance determinations in biomacromolecules by EPR spectroscopy. Q Rev Biophys 40(1):1\u201353. https:\/\/doi.org\/10.1017\/S003358350700460X","journal-title":"Q Rev Biophys"},{"issue":"3","key":"16_CR19","doi-asserted-by":"publisher","first-page":"353","DOI":"10.1042\/BJ20101871","volume":"434","author":"GW Reginsson","year":"2011","unstructured":"Reginsson GW, Schiemann O (2011) Pulsed electron-electron double resonance: beyond nanometre distance measurements on biomacromolecules. Biochem J 434(3):353\u2013363. https:\/\/doi.org\/10.1042\/BJ20101871","journal-title":"Biochem J"},{"key":"16_CR20","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/430_2012_82","volume-title":"Structural information from spin-labels and intrinsic paramagnetic centres in the biosciences","author":"PP Borbat","year":"2013","unstructured":"Borbat PP, Freed JH (2013) Pulse dipolar electron spin resonance: distance measurements. In: Timmel CR, Harmer JR (eds) Structural information from spin-labels and intrinsic paramagnetic centres in the biosciences, vol 152. Springer, Berlin, pp 1\u201382"},{"issue":"3\u20134","key":"16_CR21","doi-asserted-by":"publisher","first-page":"473","DOI":"10.1007\/BF03166213","volume":"30","author":"G Jeschke","year":"2006","unstructured":"Jeschke G, Chechik V, Ionita P et al (2006) DeerAnalysis2006\u2014a comprehensive software package for analyzing pulsed ELDOR data. Appl Magn Reson 30(3\u20134):473\u2013498. https:\/\/doi.org\/10.1007\/BF03166213","journal-title":"Appl Magn Reson"},{"key":"16_CR22","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.jmr.2012.03.006","volume":"218","author":"S Brandon","year":"2012","unstructured":"Brandon S, Beth AH, Hustedt EJ (2012) The global analysis of DEER data. J Magn Reson 218:93\u2013104. https:\/\/doi.org\/10.1016\/j.jmr.2012.03.006","journal-title":"J Magn Reson"},{"issue":"2","key":"16_CR23","doi-asserted-by":"publisher","first-page":"209","DOI":"10.5194\/mr-1-209-2020","volume":"1","author":"L F\u00e1bregas Ib\u00e1\u00f1ez","year":"2020","unstructured":"F\u00e1bregas Ib\u00e1\u00f1ez L, Jeschke G, Stoll S (2020) DeerLab: a comprehensive software package for analyzing dipolar electron paramagnetic resonance spectroscopy data. Magn Reson 1(2):209\u2013224. https:\/\/doi.org\/10.5194\/mr-1-209-2020","journal-title":"Magn Reson"},{"key":"16_CR24","doi-asserted-by":"publisher","first-page":"595","DOI":"10.1016\/bs.mie.2015.06.006","volume":"563","author":"G Hagelueken","year":"2015","unstructured":"Hagelueken G, Abdullin D, Schiemann O (2015) mtsslSuite: probing biomolecular conformation by spin-labeling studies. Methods Enzymol 563:595\u2013622. https:\/\/doi.org\/10.1016\/bs.mie.2015.06.006","journal-title":"Methods Enzymol"},{"key":"16_CR25","doi-asserted-by":"publisher","unstructured":"Polyhach Y, Bordignon E, Jeschke G (2011) Rotamer libraries of spin labelled cysteines for protein studies. Phys Chem Chem Phys 13(6):2356\u20132366. https:\/\/doi.org\/10.1039\/C0CP01865A","DOI":"10.1039\/C0CP01865A"},{"issue":"42","key":"16_CR26","doi-asserted-by":"publisher","first-page":"24282","DOI":"10.1039\/D0CP04920D","volume":"22","author":"S Spicher","year":"2020","unstructured":"Spicher S, Abdullin D, Grimme S et al (2020) Modeling of spin-spin distance distributions for nitroxide labeled biomacromolecules. Phys Chem Chem Phys 22(42):24282\u201324290. https:\/\/doi.org\/10.1039\/D0CP04920D","journal-title":"Phys Chem Chem Phys"},{"issue":"50","key":"16_CR27","doi-asserted-by":"publisher","first-page":"12148","DOI":"10.1002\/ange.201105648","volume":"123","author":"S Reckel","year":"2011","unstructured":"Reckel S, Gottstein D, Stehle J et al (2011) Solution NMR structure of Proteorhodopsin. Angew Chem 123(50):12148\u201312152. https:\/\/doi.org\/10.1002\/ange.201105648","journal-title":"Angew Chem"},{"issue":"10","key":"16_CR28","doi-asserted-by":"publisher","first-page":"936","DOI":"10.1002\/cbic.200300700","volume":"4","author":"B F\u00fcrtig","year":"2003","unstructured":"F\u00fcrtig B, Richter C, W\u00f6hnert J et al (2003) NMR spectroscopy of RNA. Chembiochem 4(10):936\u2013962. https:\/\/doi.org\/10.1002\/cbic.200300700","journal-title":"Chembiochem"},{"issue":"4","key":"16_CR29","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1261\/rna.049726.115","volume":"21","author":"E Westhof","year":"2015","unstructured":"Westhof E (2015) Twenty years of RNA crystallography. RNA 21(4):486\u2013487. https:\/\/doi.org\/10.1261\/rna.049726.115","journal-title":"RNA"},{"key":"16_CR30","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1016\/s0076-6879(00)17014-4","volume":"317","author":"JH Cate","year":"2000","unstructured":"Cate JH, Doudna JA (2000) Solving large RNA structures by X-ray crystallography. Methods Enzymol 317:169\u2013180. https:\/\/doi.org\/10.1016\/s0076-6879(00)17014-4","journal-title":"Methods Enzymol"},{"issue":"7549","key":"16_CR31","doi-asserted-by":"publisher","first-page":"640","DOI":"10.1038\/nature14427","volume":"520","author":"H Khatter","year":"2015","unstructured":"Khatter H, Myasnikov AG, Natchiar SK et al (2015) Structure of the human 80S ribosome. Nature 520(7549):640\u2013645. https:\/\/doi.org\/10.1038\/nature14427","journal-title":"Nature"},{"issue":"6483","key":"16_CR32","doi-asserted-by":"publisher","first-page":"1260","DOI":"10.1126\/science.abb2507","volume":"367","author":"D Wrapp","year":"2020","unstructured":"Wrapp D, Wang N, Corbett KS et al (2020) Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science 367(6483):1260\u20131263. https:\/\/doi.org\/10.1126\/science.abb2507","journal-title":"Science"},{"key":"16_CR33","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/j.ymeth.2016.02.004","volume":"103","author":"JD Stephenson","year":"2016","unstructured":"Stephenson JD, Kenyon JC, Symmons MF et al (2016) Characterizing 3D RNA structure by single molecule FRET. Methods 103:57\u201367. https:\/\/doi.org\/10.1016\/j.ymeth.2016.02.004","journal-title":"Methods"},{"key":"16_CR34","doi-asserted-by":"publisher","DOI":"10.1007\/978-0-387-46312-4","volume-title":"Principles of fluorescence spectroscopy","author":"JR Lakowicz","year":"2006","unstructured":"Lakowicz JR (2006) Principles of fluorescence spectroscopy, 3rd edn. Springer, New York, NY","edition":"3"},{"issue":"22","key":"16_CR35","doi-asserted-by":"publisher","first-page":"11850","DOI":"10.1093\/nar\/gkz1039","volume":"47","author":"AA Malygin","year":"2019","unstructured":"Malygin AA, Krumkacheva OA, Graifer DM et al (2019) Exploring the interactions of short RNAs with the human 40S ribosomal subunit near the mRNA entry site by EPR spectroscopy. Nucleic Acids Res 47(22):11850\u201311860. https:\/\/doi.org\/10.1093\/nar\/gkz1039","journal-title":"Nucleic Acids Res"},{"issue":"40","key":"16_CR36","doi-asserted-by":"publisher","first-page":"E2675","DOI":"10.1073\/pnas.1202286109","volume":"109","author":"C Pliotas","year":"2012","unstructured":"Pliotas C, Ward R, Branigan E et al (2012) Conformational state of the MscS mechanosensitive channel in solution revealed by pulsed electron-electron double resonance (PELDOR) spectroscopy. Proc Natl Acad Sci U S A 109(40):E2675\u2013E2682. https:\/\/doi.org\/10.1073\/pnas.1202286109","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"16_CR37","doi-asserted-by":"publisher","first-page":"954","DOI":"10.1093\/nar\/gkv1373","volume":"44","author":"D Constantinescu-Aruxandei","year":"2016","unstructured":"Constantinescu-Aruxandei D, Petrovic-Stojanovska B, Schiemann O et al (2016) Taking a molecular motor for a spin: helicase mechanism studied by spin labeling and PELDOR. Nucleic Acids Res 44(2):954\u2013968. https:\/\/doi.org\/10.1093\/nar\/gkv1373","journal-title":"Nucleic Acids Res"},{"issue":"7502","key":"16_CR38","doi-asserted-by":"publisher","first-page":"588","DOI":"10.1038\/nature13271","volume":"509","author":"O Duss","year":"2014","unstructured":"Duss O, Michel E, Yulikov M et al (2014) Structural basis of the non-coding RNA RsmZ acting as a protein sponge. Nature 509(7502):588\u2013592. https:\/\/doi.org\/10.1038\/nature13271","journal-title":"Nature"},{"key":"16_CR39","doi-asserted-by":"publisher","first-page":"3669","DOI":"10.1038\/ncomms4669","volume":"5","author":"O Duss","year":"2014","unstructured":"Duss O, Yulikov M, Jeschke G et al (2014) EPR-aided approach for solution structure determination of large RNAs or protein-RNA complexes. Nat Commun 5:3669. https:\/\/doi.org\/10.1038\/ncomms4669","journal-title":"Nat Commun"},{"issue":"4","key":"16_CR40","doi-asserted-by":"publisher","first-page":"834","DOI":"10.1016\/j.bpj.2014.01.008","volume":"106","author":"R Ward","year":"2014","unstructured":"Ward R, Pliotas C, Branigan E et al (2014) Probing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonance. Biophys J 106(4):834\u2013842. https:\/\/doi.org\/10.1016\/j.bpj.2014.01.008","journal-title":"Biophys J"},{"issue":"38","key":"16_CR41","doi-asserted-by":"publisher","first-page":"11538","DOI":"10.1002\/anie.201606335","volume":"55","author":"B Joseph","year":"2016","unstructured":"Joseph B, Tormyshev VM, Rogozhnikova OY et al (2016) Selective high-resolution detection of membrane protein-ligand interaction in native membranes using trityl-nitroxide PELDOR. Angew Chem Int Ed Engl 55(38):11538\u201311542. https:\/\/doi.org\/10.1002\/anie.201606335","journal-title":"Angew Chem Int Ed Engl"},{"issue":"5","key":"16_CR42","doi-asserted-by":"publisher","first-page":"1213","DOI":"10.1016\/j.bpj.2015.01.015","volume":"108","author":"V Meyer","year":"2015","unstructured":"Meyer V, Swanson MA, Clouston LJ et al (2015) Room-temperature distance measurements of immobilized spin-labeled protein by DEER\/PELDOR. Biophys J 108(5):1213\u20131219. https:\/\/doi.org\/10.1016\/j.bpj.2015.01.015","journal-title":"Biophys J"},{"issue":"33","key":"16_CR43","doi-asserted-by":"publisher","first-page":"10540","DOI":"10.1002\/anie.201803682","volume":"57","author":"M Gr\u00e4nz","year":"2018","unstructured":"Gr\u00e4nz M, Erlenbach N, Spindler P et al (2018) Dynamics of nucleic acids at room temperature revealed by pulsed EPR spectroscopy. Angew Chem Int Ed Engl 57(33):10540\u201310543. https:\/\/doi.org\/10.1002\/anie.201803682","journal-title":"Angew Chem Int Ed Engl"},{"issue":"34","key":"16_CR44","doi-asserted-by":"publisher","first-page":"11674","DOI":"10.1021\/jacs.7b05363","volume":"139","author":"LS Stelzl","year":"2017","unstructured":"Stelzl LS, Erlenbach N, Heinz M et al (2017) Resolving the conformational dynamics of DNA with \u00c5ngstrom resolution by pulsed electron-electron double resonance and molecular dynamics. J Am Chem Soc 139(34):11674\u201311677. https:\/\/doi.org\/10.1021\/jacs.7b05363","journal-title":"J Am Chem Soc"},{"issue":"6","key":"16_CR45","doi-asserted-by":"publisher","first-page":"544","DOI":"10.1080\/00268976.2014.960494","volume":"113","author":"D Abdullin","year":"2015","unstructured":"Abdullin D, Hagelueken G, Hunter RI et al (2015) Geometric model-based fitting algorithm for orientation-selective PELDOR data. Mol Phys 113(6):544\u2013560. https:\/\/doi.org\/10.1080\/00268976.2014.960494","journal-title":"Mol Phys"},{"issue":"16","key":"16_CR46","doi-asserted-by":"publisher","first-page":"2904","DOI":"10.1002\/anie.200805758","volume":"48","author":"G Hagelueken","year":"2009","unstructured":"Hagelueken G, Ingledew WJ, Huang H et al (2009) PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein Wza from Escherichia coli. Angew Chem Int Ed Engl 48(16):2904\u20132906. https:\/\/doi.org\/10.1002\/anie.200805758","journal-title":"Angew Chem Int Ed Engl"},{"issue":"14","key":"16_CR47","doi-asserted-by":"publisher","first-page":"4700","DOI":"10.1002\/chem.201505143","volume":"22","author":"S Valera","year":"2016","unstructured":"Valera S, Ackermann K, Pliotas C et al (2016) Accurate extraction of nanometer distances in multimers by pulse EPR. Chemistry 22(14):4700\u20134703. https:\/\/doi.org\/10.1002\/chem.201505143","journal-title":"Chemistry"},{"key":"16_CR48","doi-asserted-by":"publisher","unstructured":"Hett T, Zbik T, Mukherjee S, Matsuoka H, B\u00f6nigk W, Klose D, Rouillon C, Brenner N, Peuker S, Klement R, Steinhoff H-J, Grubm\u00fcller H, Seifert R, Schiemann O, Kaupp UB (2021) Spatiotemporal resolution of conformational changes in biomolecules by combining pulsed electron\u2013electron double resonance spectroscopy with microsecond freeze-hyperquenching.. J Am Chem Soc 143(18):6981-6989. https:\/\/doi.org\/10.1021\/jacs.1c01081","DOI":"10.1021\/jacs.1c01081"},{"key":"16_CR49","doi-asserted-by":"publisher","unstructured":"Schiemann O, Heubach CA, Abdullin D, Ackermann K, Azarkh M, Bagryanskaya EG, Drescher M, Endeward B, Freed JH, Galazzo L, Goldfarb D, Hett T, Esteban Hofer L, F\u00e1bregas Ib\u00e1\u00f1ez L, Hustedt EJ, Kucher S, Kuprov I, Lovett JE, Meyer A, Ruthstein S, Saxena S, Stoll S, Timmel CR, Di Valentin M, Mchaourab HS, Prisner TF, Bode BE, Bordignon E, Bennati M, Jeschke G (2021) Benchmark test and guidelines for DEER\/PELDOR experiments on nitroxide-labeled biomolecules. J Am Chem Soc 143(43):17875\u201317890. https:\/\/doi.org\/10.1021\/jacs.1c07371","DOI":"10.1021\/jacs.1c07371"},{"key":"16_CR50","unstructured":"Jeschke G (2019) DeerAnalysis 2019. https:\/\/epr.ethz.ch\/software.html. Accessed 11 Jan 2021"},{"issue":"8","key":"16_CR51","doi-asserted-by":"publisher","first-page":"eaat5218","DOI":"10.1126\/sciadv.aat5218","volume":"4","author":"SG Worswick","year":"2018","unstructured":"Worswick SG, Spencer JA, Jeschke G et al (2018) Deep neural network processing of DEER data. Sci Adv 4(8):eaat5218. https:\/\/doi.org\/10.1126\/sciadv.aat5218","journal-title":"Sci Adv"},{"key":"16_CR52","unstructured":"Vicino MF, Wuebben C, Kerzhner M, Famulok M, Schiemann O. Spin labeling of long RNAs via click reaction and enzymatic ligation. Methods Mol Biol"},{"key":"16_CR53","unstructured":"Bruker BioSpin GmbH, EPR Division (2014) Product description: ER 5106QT-2 Q-Band Probehead"},{"key":"16_CR54","unstructured":"Hett T (2020) PELDOR_PulseSPEL. https:\/\/github.com\/TobiasHett\/PELDOR_PulseSPEL. Accessed 11 Jan 2021"},{"issue":"25","key":"16_CR55","doi-asserted-by":"publisher","first-page":"5782","DOI":"10.1021\/bi900781u","volume":"48","author":"H Ghimire","year":"2009","unstructured":"Ghimire H, McCarrick RM, Budil DE et al (2009) Significantly improved sensitivity of Q-band PELDOR\/DEER experiments relative to X-band is observed in measuring the intercoil distance of a leucine zipper motif peptide (GCN4-LZ). Biochemistry 48(25):5782\u20135784. https:\/\/doi.org\/10.1021\/bi900781u","journal-title":"Biochemistry"},{"issue":"42","key":"16_CR56","doi-asserted-by":"publisher","first-page":"15246","DOI":"10.1021\/ja904808n","volume":"131","author":"B Endeward","year":"2009","unstructured":"Endeward B, Butterwick JA, MacKinnon R et al (2009) Pulsed electron-electron double-resonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA. J Am Chem Soc 131(42):15246\u201315250. https:\/\/doi.org\/10.1021\/ja904808n","journal-title":"J Am Chem Soc"},{"key":"16_CR57","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1007\/978-0-387-49367-1_2","volume-title":"ESR spectroscopy in membrane biophysics","author":"G Jeschke","year":"2007","unstructured":"Jeschke G (2007) Instrumentation and experimental setup. In: ESR spectroscopy in membrane biophysics, vol 27. Springer US, Boston, MA, pp 17\u201347"},{"key":"16_CR58","unstructured":"Hett T (2020) ScanState. https:\/\/github.com\/TobiasHett\/ScanState. Accessed 11 Jan 2021"},{"key":"16_CR59","unstructured":"Hett T (2020) DTA2dat. https:\/\/github.com\/TobiasHett\/DTA2dat. Accessed 11 Jan 2021"},{"issue":"1","key":"16_CR60","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1016\/j.jmr.2005.08.013","volume":"178","author":"S Stoll","year":"2006","unstructured":"Stoll S, Schweiger A (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J Magn Reson 178(1):42\u201355. https:\/\/doi.org\/10.1016\/j.jmr.2005.08.013","journal-title":"J Magn Reson"},{"key":"16_CR61","unstructured":"Altenbach C (2020) LongDistances. https:\/\/sites.google.com\/site\/altenbach\/labview-programs\/epr-programs\/long-distances. Accessed 22 Jan 2021"},{"issue":"6","key":"16_CR62","doi-asserted-by":"publisher","first-page":"3287","DOI":"10.1016\/S0006-3495(97)78353-X","volume":"73","author":"HJ Steinhoff","year":"1997","unstructured":"Steinhoff HJ, Radzwill N, Thevis W et al (1997) Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure. Biophys J 73(6):3287\u20133298. https:\/\/doi.org\/10.1016\/S0006-3495(97)78353-X","journal-title":"Biophys J"},{"key":"16_CR63","unstructured":"Jeschke G, Stoll S (2019) DeerAnalysis User Manual - Version 2019. http:\/\/www.epr.ethz.ch\/software\/index. Accessed 11 Jan 2021"},{"key":"16_CR64","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1093\/nar\/28.1.235","volume":"28","author":"HM Berman","year":"2000","unstructured":"Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE (2000) The Protein Data Bank. Nucleic Acids Res 28:235\u2013242. https:\/\/www.rcsb.org","journal-title":"Nucleic Acids Res"},{"issue":"3","key":"16_CR65","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1007\/s00723-012-0314-0","volume":"42","author":"G Hagelueken","year":"2012","unstructured":"Hagelueken G, Ward R, Naismith JH et al (2012) MtsslWizard: in silico spin-labeling and generation of distance distributions in PyMOL. Appl Magn Reson 42(3):377\u2013391. https:\/\/doi.org\/10.1007\/s00723-012-0314-0","journal-title":"Appl Magn Reson"},{"key":"16_CR66","doi-asserted-by":"publisher","first-page":"14388","DOI":"10.1002\/chem.201902908","volume":"25","author":"D Abdullin","year":"2019","unstructured":"Abdullin D, Brehm P, Fleck N, Spicher S, Grimme S, Schiemann O (2019) Pulsed EPR dipolar spectroscopy on spin pairs with one highly anisotropic spin center: the low-spin Fe(III) case. Chem Eur J 25:14388\u201314398. https:\/\/github.com\/dinarabdullin\/SnrCalculator","journal-title":"Chem Eur J"},{"issue":"12","key":"16_CR67","doi-asserted-by":"publisher","first-page":"1224","DOI":"10.1002\/cphc.202000312","volume":"21","author":"T Schmidt","year":"2020","unstructured":"Schmidt T, Jeon J, Okuno Y et al (2020) Submillisecond freezing permits cryoprotectant-free EPR double electron-electron resonance spectroscopy. ChemPhysChem 21(12):1224\u20131229. https:\/\/doi.org\/10.1002\/cphc.202000312","journal-title":"ChemPhysChem"},{"issue":"18","key":"16_CR68","doi-asserted-by":"publisher","first-page":"10518","DOI":"10.1093\/nar\/gkaa703","volume":"48","author":"C Wuebben","year":"2020","unstructured":"Wuebben C, Vicino MF, Mueller M et al (2020) Do the P1 and P2 hairpins of the guanidine-II riboswitch interact? Nucleic Acids Res 48(18):10518\u201310526. https:\/\/doi.org\/10.1093\/nar\/gkaa703","journal-title":"Nucleic Acids Res"},{"issue":"6","key":"16_CR69","doi-asserted-by":"publisher","first-page":"1827","DOI":"10.1002\/anie.201410396","volume":"54","author":"D Abdullin","year":"2015","unstructured":"Abdullin D, Florin N, Hagelueken G et al (2015) EPR-based approach for the localization of paramagnetic metal ions in biomolecules. Angew Chem Int Ed Engl 54(6):1827\u20131831. https:\/\/doi.org\/10.1002\/anie.201410396","journal-title":"Angew Chem Int Ed Engl"},{"key":"16_CR70","unstructured":"Weber RT (2005) ELEXSYS E580 User\u2019s Manual. Bruker BioSpin Corporation, Manual Version 2.0"},{"issue":"7","key":"16_CR71","doi-asserted-by":"publisher","first-page":"5134","DOI":"10.1063\/1.464916","volume":"98","author":"RG Larsen","year":"1993","unstructured":"Larsen RG, Singel DJ (1993) Double electron\u2013electron resonance spin\u2013echo modulation: spectroscopic measurement of electron spin pair separations in orientationally disordered solids. J Chem Phys 98(7):5134\u20135146. https:\/\/doi.org\/10.1063\/1.464916","journal-title":"J Chem Phys"},{"key":"16_CR72","doi-asserted-by":"publisher","first-page":"1116","DOI":"10.1007\/978-3-642-16712-6_662","volume-title":"Encyclopedia of biophysics","author":"R Ward","year":"2013","unstructured":"Ward R, Schiemann O (2013) Interspin distance determination by EPR. In: Roberts GCK (ed) Encyclopedia of biophysics. Springer, Berlin, pp 1116\u20131123"},{"issue":"6","key":"16_CR73","doi-asserted-by":"publisher","first-page":"64102","DOI":"10.1063\/1.3073040","volume":"130","author":"A Marko","year":"2009","unstructured":"Marko A, Margraf D, Yu H et al (2009) Molecular orientation studies by pulsed electron-electron double resonance experiments. J Chem Phys 130(6):64102. https:\/\/doi.org\/10.1063\/1.3073040","journal-title":"J Chem Phys"},{"key":"16_CR74","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/j.jmr.2014.12.008","volume":"252","author":"TF Prisner","year":"2015","unstructured":"Prisner TF, Marko A, Sigurdsson ST (2015) Conformational dynamics of nucleic acid molecules studied by PELDOR spectroscopy with rigid spin labels. J Magn Reson 252:187\u2013198. https:\/\/doi.org\/10.1016\/j.jmr.2014.12.008","journal-title":"J Magn Reson"},{"key":"16_CR75","first-page":"1459","volume-title":"eMagRes","author":"G Jeschke","year":"2007","unstructured":"Jeschke G (2007) Dipolar spectroscopy - double-resonance methods. In: Harris RK, Wasylishen RL (eds) eMagRes. Wiley, Chichester, pp 1459\u20131476"},{"key":"16_CR76","first-page":"187","volume-title":"eMagRes","author":"E Reijerse","year":"2007","unstructured":"Reijerse E, Savitsky A (2007) Electron paramagnetic resonance instrumentation. In: Harris RK, Wasylishen RL (eds) eMagRes. Wiley, Chichester, pp 187\u2013206"}],"container-title":["Methods in Molecular Biology","DNAzymes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-0716-2047-2_16","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,18]],"date-time":"2023-11-18T05:13:08Z","timestamp":1700284388000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/978-1-0716-2047-2_16"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022]]},"ISBN":["9781071620465","9781071620472"],"references-count":76,"URL":"https:\/\/doi.org\/10.1007\/978-1-0716-2047-2_16","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"value":"1064-3745","type":"print"},{"value":"1940-6029","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022]]},"assertion":[{"value":"28 February 2022","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}