{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,16]],"date-time":"2026-04-16T03:04:36Z","timestamp":1776308676400,"version":"3.50.1"},"reference-count":62,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[1998,6,1]],"date-time":"1998-06-01T00:00:00Z","timestamp":896659200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[1998,6]]},"DOI":"10.1006\/jmbi.1998.1811","type":"journal-article","created":{"date-parts":[[2002,10,7]],"date-time":"2002-10-07T11:22:43Z","timestamp":1033989763000},"page":"929-943","source":"Crossref","is-referenced-by-count":29,"title":["A disorder-to-order transition coupled to DNA binding in the essential zinc-finger DNA-binding domain of yeast ADR1"],"prefix":"10.1006","volume":"279","author":[{"given":"David E","family":"Hyre","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rachel E","family":"Klevit","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1006\/jmbi.1998.1811_BIB1","doi-asserted-by":"crossref","first-page":"9832","DOI":"10.1021\/ja00074a073","article-title":"NMR order parameters and free energy","volume":"115","author":"Akke","year":"1993","journal-title":"J. Am. Chem. Soc."},{"key":"10.1006\/jmbi.1998.1811_BIB2","doi-asserted-by":"crossref","first-page":"8686","DOI":"10.1021\/bi970872m","article-title":"Microsecond protein folding kinetics from native-state hydrogen exchange","volume":"36","author":"Arrington","year":"1997","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB3","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1002\/prot.340170110","article-title":"Primary structure effects on peptide group hydrogen exchange","volume":"17","author":"Bai","year":"1993","journal-title":"Proteins"},{"key":"10.1006\/jmbi.1998.1811_BIB4","doi-asserted-by":"crossref","first-page":"5269","DOI":"10.1021\/bi00138a005","article-title":"Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy","volume":"31","author":"Barbato","year":"1992","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB5","doi-asserted-by":"crossref","first-page":"4460","DOI":"10.1021\/bi00181a005","article-title":"Structure of a histidine-X4-histidine zinc finger domain","volume":"33","author":"Bernstein","year":"1994","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB6","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/328443a0","article-title":"Two zinc fingers of a yeast regulatory protein shown by genetic evidence to be essential for its function","volume":"328","author":"Blumberg","year":"1987","journal-title":"Nature"},{"key":"10.1006\/jmbi.1998.1811_BIB7","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1126\/science.7754375","article-title":"Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling","volume":"268","author":"Br\u00fcschweiler","year":"1995","journal-title":"Science"},{"key":"10.1006\/jmbi.1998.1811_BIB8","doi-asserted-by":"crossref","first-page":"3842","DOI":"10.1128\/MCB.14.6.3842","article-title":"Identification of potential target genes for Adr1p through characterization of essential nucleotides in UAS1","volume":"14","author":"Cheng","year":"1994","journal-title":"Mol. Cell. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB9","doi-asserted-by":"crossref","first-page":"7387","DOI":"10.1021\/bi00484a006","article-title":"Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy","volume":"29","author":"Clore","year":"1990","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB10","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1002\/pro.5560040505","article-title":"Backbone dynamics of the oligomerization domain of p53 determined from 15N NMR relaxation measurements","volume":"4","author":"Clubb","year":"1995","journal-title":"Protein Sci."},{"key":"10.1006\/jmbi.1998.1811_BIB11","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1007\/BF00200435","article-title":"Secondary structure of beta-hydroxydecanoyl thiol ester dehydrase, a 39-kDa protein, derived from H alpha, C alpha, C beta and CO signal assignments and the chemical shift index","volume":"7","author":"Copi\u00e9","year":"1996","journal-title":"J. Biomol. NMR"},{"key":"10.1006\/jmbi.1998.1811_BIB12","doi-asserted-by":"crossref","first-page":"7739","DOI":"10.1021\/bi00081a019","article-title":"Cold denaturation-induced conformational changes in phosphoglycerate kinase from yeast","volume":"32","author":"Damaschun","year":"1993","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB13","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1002\/pro.5560051218","article-title":"NMR studies of structure, hydrogen exchange, and main-chain dynamics in a disrupted-core mutant of thioredoxin","volume":"5","author":"deLorimier","year":"1996","journal-title":"Protein Sci."},{"key":"10.1006\/jmbi.1998.1811_BIB14","series-title":"Probability and Statistics for Engineering and the Physical Sciences","author":"Devore","year":"1982"},{"key":"10.1006\/jmbi.1998.1811_BIB15","doi-asserted-by":"crossref","first-page":"5984","DOI":"10.1021\/bi00185a040","article-title":"Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation","volume":"33","author":"Farrow","year":"1994","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB16","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1021\/bi00003a021","article-title":"Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer","volume":"34","author":"Farrow","year":"1995","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB17","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1007\/BF00211779","article-title":"Spectral density function mapping using 15N relaxation data exclusively","volume":"6","author":"Farrow","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1006\/jmbi.1998.1811_BIB18","doi-asserted-by":"crossref","first-page":"8439","DOI":"10.1021\/bi952932z","article-title":"Base-catalysis of imino proton exchange in DNA","volume":"35","author":"Folta-Stogniew","year":"1996","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB19","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1038\/nsb0897-605","article-title":"Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA","volume":"4","author":"Foster","year":"1997","journal-title":"Nature Struct. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB20","doi-asserted-by":"crossref","first-page":"12593","DOI":"10.1021\/ja00079a052","article-title":"The importance of not saturating H2O in protein NMR. Application to sensitivity enhancement and NOE measurements","volume":"115","author":"Grzesiek","year":"1993","journal-title":"J. Am. Chem. Soc."},{"key":"10.1006\/jmbi.1998.1811_BIB21","doi-asserted-by":"crossref","first-page":"9335","DOI":"10.1021\/bi952524v","article-title":"Backbone dynamics, amide hydrogen exchange, and resonance assignments of the DNA methylphosphotriester repair domain ofEscherichia coli Ada using NMR","volume":"35","author":"Habazettl","year":"1996","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB22","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1002\/pro.5560020609","article-title":"Structures of DNA-binding mutant zinc finger domains","volume":"2","author":"Hoffman","year":"1993","journal-title":"Protein Sci."},{"key":"10.1006\/jmbi.1998.1811_BIB23","first-page":"299","article-title":"A discussion of the pH dependence of the hydrogen-deuterium exchange of proteins","volume":"34","author":"Hvidt","year":"1964","journal-title":"Compt. Rend. Trav. Lab. Carlsberg"},{"key":"10.1006\/jmbi.1998.1811_BIB25","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0076-6879(94)40040-7","article-title":"Use of least-squares techniques in biochemistry","volume":"240","author":"Johnson","year":"1994","journal-title":"Methods Enzymol."},{"key":"10.1006\/jmbi.1998.1811_BIB26","doi-asserted-by":"crossref","first-page":"3913","DOI":"10.1093\/nar\/5.10.3913","article-title":"Pulsed FT-NMR double resonance studies of yeast tRNAPhe","volume":"5","author":"Johnston","year":"1978","journal-title":"Nucl. Acids Res."},{"key":"10.1006\/jmbi.1998.1811_BIB27","doi-asserted-by":"crossref","first-page":"8972","DOI":"10.1021\/bi00449a003","article-title":"Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy","volume":"28","author":"Kay","year":"1989","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB28","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1126\/science.276.5315.1112","article-title":"Folding-unfolding transitions in single titin molecules characterized with laser tweezers","volume":"276","author":"Kellermayer","year":"1997","journal-title":"Science"},{"key":"10.1006\/jmbi.1998.1811_BIB29","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1023\/A:1018631009583","article-title":"Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13 Canuclear spin relaxation","volume":"9","author":"Lee","year":"1997","journal-title":"J. Biomol. NMR"},{"key":"10.1006\/jmbi.1998.1811_BIB30","doi-asserted-by":"crossref","first-page":"2674","DOI":"10.1021\/bi9526802","article-title":"Internal mobility in the partially folded DNA binding and dimerization domains of GAL4","volume":"35","author":"Lefevre","year":"1996","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB31","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1006\/jmrb.1994.1098","article-title":"Overcoming solvent saturation-transfer artifacts in protein NMR at neutral pH. Application of pulsed field gradients in measurements of 1H-15N Overhauser effects","volume":"105","author":"Li","year":"1994","journal-title":"J. Magn. Reson. Ser. B"},{"key":"10.1006\/jmbi.1998.1811_BIB32","doi-asserted-by":"crossref","first-page":"2408","DOI":"10.1021\/bi00008a003","article-title":"Human type-alpha transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by nitrogen-15 relaxation measurements","volume":"34","author":"Li","year":"1995","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB33","doi-asserted-by":"crossref","first-page":"2647","DOI":"10.1002\/pro.5560051228","article-title":"Insights into the local residual entropy of proteins provided by NMR relaxation","volume":"5","author":"Li","year":"1996","journal-title":"Protein Sci."},{"key":"10.1006\/jmbi.1998.1811_BIB36","doi-asserted-by":"crossref","first-page":"7305","DOI":"10.1021\/bi963161h","article-title":"Anisotropic molecular rotational diffusion in 15N spin relaxation studies of protein mobility","volume":"36","author":"Luginb\u00fchl","year":"1997","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB37","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1021\/bi951933o","article-title":"Local mobility within villin 14 T probed via heteronuclear relaxation measurements and a reduced spectral density mapping","volume":"35","author":"Markus","year":"1996","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB38","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1038\/nsb0495-274","article-title":"Flexibility and function in HIV-1 protease","volume":"2","author":"Nicholson","year":"1995","journal-title":"Nature Struct. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB39","doi-asserted-by":"crossref","first-page":"4371","DOI":"10.1021\/ja00012a001","article-title":"Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance 13C heteronuclear NMR spectroscopy","volume":"113","author":"Palmer","year":"1991","journal-title":"J. Am. Chem. Soc."},{"key":"10.1006\/jmbi.1998.1811_BIB40","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1073\/pnas.87.1.137","article-title":"Spectroscopic studies of wild-type and mutant \u201czinc finger\u201d peptides","volume":"87","author":"P\u00e1rraga","year":"1990","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1006\/jmbi.1998.1811_BIB41","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1126\/science.2028256","article-title":"Zinc finger-DNA recognition","volume":"252","author":"Pavletich","year":"1991","journal-title":"Science"},{"key":"10.1006\/jmbi.1998.1811_BIB42","doi-asserted-by":"crossref","first-page":"8571","DOI":"10.1021\/bi00151a027","article-title":"Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments","volume":"31","author":"Peng","year":"1992","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB43","doi-asserted-by":"crossref","first-page":"16733","DOI":"10.1021\/bi00051a023","article-title":"Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields","volume":"34","author":"Peng","year":"1995","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB44","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1007\/BF02192855","article-title":"Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions","volume":"2","author":"Piotto","year":"1992","journal-title":"J. Biomol. NMR"},{"key":"10.1006\/jmbi.1998.1811_BIB45","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/S0959-440X(94)90056-6","article-title":"Zinc finger diversity","volume":"4","author":"Schmiedeskamp","year":"1994","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB46","doi-asserted-by":"crossref","first-page":"14003","DOI":"10.1021\/bi971364f","article-title":"Paramagnetic cobalt as a probe of the orientation of an accessory DNA-binding region of the yeast ADR1 zinc-finger protein","volume":"36","author":"Schmiedeskamp","year":"1997","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB47","doi-asserted-by":"crossref","first-page":"1835","DOI":"10.1002\/pro.5560060904","article-title":"NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1","volume":"6","author":"Schmiedeskamp","year":"1997","journal-title":"Protein Sci."},{"key":"10.1006\/jmbi.1998.1811_BIB48","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1128\/MCB.6.6.1894","article-title":"ADR1\u2013mediated regulation of ADH2 requires an inverted repeat sequence","volume":"6","author":"Shuster","year":"1986","journal-title":"Mol. Cell. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB49","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1128\/MCB.11.2.699","article-title":"The Saccharomyces cerevisiae ADR1 gene is a positive regulator of transcription of genes encoding peroxisomal proteins","volume":"11","author":"Simon","year":"1991","journal-title":"Mol. Cell. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB50","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1021\/bi961670d","article-title":"Backbone and side chain dynamics of lac repressor headpiece (1\u201356) and its complex with DNA","volume":"36","author":"Slijper","year":"1997","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB51","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/BF01877227","article-title":"Measurement of the exchange rates of rapidly exchanging amide protons","volume":"1","author":"Spera","year":"1991","journal-title":"J. Biomol. NMR"},{"key":"10.1006\/jmbi.1998.1811_BIB52","doi-asserted-by":"crossref","first-page":"4394","DOI":"10.1021\/bi00133a003","article-title":"Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurements","volume":"31","author":"Stone","year":"1992","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB53","doi-asserted-by":"crossref","first-page":"2360","DOI":"10.1128\/MCB.9.6.2360","article-title":"Localization of a minimal binding domain and activation regions in yeast regulatory protein ADR1","volume":"9","author":"Thukral","year":"1989","journal-title":"Mol. Cell. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB54","doi-asserted-by":"crossref","first-page":"1566","DOI":"10.1128\/MCB.11.3.1566","article-title":"Two monomers of yeast transcription factor ADR1 bind a palindromic sequence symmetrically to activate ADH2 expression","volume":"11","author":"Thukral","year":"1991","journal-title":"Mol. Cell. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB55","doi-asserted-by":"crossref","first-page":"9188","DOI":"10.1073\/pnas.88.20.9188","article-title":"Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1","volume":"88","author":"Thukral","year":"1991","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1006\/jmbi.1998.1811_BIB56","doi-asserted-by":"crossref","first-page":"1014","DOI":"10.1111\/j.1432-1033.1995.tb20650.x","article-title":"Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements","volume":"230","author":"Tjandra","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"10.1006\/jmbi.1998.1811_BIB57","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/BF00410326","article-title":"Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation measurements at two magnetic fields","volume":"8","author":"Tjandra","year":"1996","journal-title":"J. Biomol. NMR"},{"key":"10.1006\/jmbi.1998.1811_BIB58","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/BF00175245","article-title":"The 13C chemical-shift index","volume":"4","author":"Wishart","year":"1994","journal-title":"J. Biomol. NMR"},{"key":"10.1006\/jmbi.1998.1811_BIB59","series-title":"NMR of Proteins and Nucleic Acids","author":"W\u00fcthrich","year":"1986"},{"key":"10.1006\/jmbi.1998.1811_BIB60","doi-asserted-by":"crossref","first-page":"3365","DOI":"10.1021\/bi00228a003","article-title":"ADR1a, a zinc finger peptide, exists in two folded conformations","volume":"30","author":"Xu","year":"1991","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB61","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1006\/jmbi.1997.1285","article-title":"Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation","volume":"272","author":"Yang","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1006\/jmbi.1998.1811_BIB62","doi-asserted-by":"crossref","first-page":"8453","DOI":"10.1021\/bi00194a009","article-title":"Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein","volume":"33","author":"Zink","year":"1994","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB24","doi-asserted-by":"crossref","first-page":"3162","DOI":"10.1021\/bi00010a005","article-title":"Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei","volume":"34","author":"Ishima","year":"1995","journal-title":"Biochemistry"},{"key":"10.1006\/jmbi.1998.1811_BIB34","doi-asserted-by":"crossref","first-page":"4546","DOI":"10.1021\/ja00381a009","article-title":"Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity","volume":"104","author":"Lipari","year":"1982","journal-title":"J. Am. Chem. Soc."},{"key":"10.1006\/jmbi.1998.1811_BIB35","doi-asserted-by":"crossref","first-page":"4559","DOI":"10.1021\/ja00381a010","article-title":"Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results","volume":"104","author":"Lipari","year":"1982","journal-title":"J. Am. Chem. Soc."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283698918113?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283698918113?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,5,7]],"date-time":"2019-05-07T00:22:57Z","timestamp":1557188577000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283698918113"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,6]]},"references-count":62,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1998,6]]}},"alternative-id":["S0022283698918113"],"URL":"https:\/\/doi.org\/10.1006\/jmbi.1998.1811","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[1998,6]]}}}