{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T13:10:23Z","timestamp":1785157823961,"version":"3.55.0"},"reference-count":47,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2009,1,1]],"date-time":"2009-01-01T00:00:00Z","timestamp":1230768000000},"content-version":"vor","delay-in-days":1492,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2004,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Infrequent structural fluctuations of a globular protein is seldom detected and studied in detail. One tyrosine ring of HPr from <jats:italic>Staphylococcus carnosus<\/jats:italic>, an 88\u2010residue phosphocarrier protein with no disulfide bonds, undergoes a very slow ring flip, the pressure and temperature dependence of which is studied in detail using the on\u2010line cell high\u2010pressure nuclear magnetic resonance technique in the pressure range from 3 MPa to 200 MPa and in the temperature range from 257 K to 313 K. The ring of Tyr6 is buried sandwiched between a \u03b2\u2010sheet and \u03b1\u2010helices (the water\u2010accessible area is less than 0.26 nm<jats:sup>2<\/jats:sup>), its hydroxyl proton being involved in an internal hydrogen bond. The ring flip rates10<jats:sup>1<\/jats:sup>\u223c10<jats:sup>5<\/jats:sup> s<jats:sup>\u22121<\/jats:sup> were determined from the line shape analysis of H<jats:sup>\u03b41, \u03b42<\/jats:sup> and H<jats:sup>\u03b51,\u03b52<\/jats:sup> of Tyr6, giving an activation volume \u0394<jats:italic>V<\/jats:italic><jats:sup>\u2021<\/jats:sup> of 0.044 \u00b1 0.008 nm<jats:sup>3<\/jats:sup> (27 mL mol<jats:sup>\u22121<\/jats:sup>), an activation enthalpy \u0394<jats:italic>H<\/jats:italic><jats:sup>\u2021<\/jats:sup> of 89 \u00b1 10 kJ mol<jats:sup>\u22121<\/jats:sup>, and an activation entropy \u0394<jats:italic>S<\/jats:italic><jats:sup>\u2021<\/jats:sup> of 16 \u00b1 2 JK<jats:sup>\u22121<\/jats:sup> mol<jats:sup>\u22121<\/jats:sup>. The \u0394<jats:italic>V<\/jats:italic><jats:sup>\u2021<\/jats:sup> and \u0394<jats:italic>H<\/jats:italic><jats:sup>\u2021<\/jats:sup> values for HPr found previously for Tyr and Phe ring flips of BPTI and cytochrome <jats:italic>c<\/jats:italic> fall within the range of \u0394<jats:italic>V<\/jats:italic><jats:sup>\u2021<\/jats:sup> of 28 to 51 mL mol<jats:sup>\u22121<\/jats:sup> and \u0394<jats:italic>H<\/jats:italic><jats:sup>\u2021<\/jats:sup> of 71 to 155 kJ mol<jats:sup>\u22121<\/jats:sup>. The fairly common \u0394<jats:italic>V<\/jats:italic><jats:sup>\u2021<\/jats:sup> and \u0394<jats:italic>H<\/jats:italic><jats:sup>\u2021<\/jats:sup> values are considered to represent the extra space or cavity required for the ring flip and the extra energy required to create a cavity, respectively, in the core part of a globular protein. Nearly complete cold denaturation was found to take place at 200 MPa and 257 K independently from the ring reorientation process.<\/jats:p>","DOI":"10.1110\/ps.04877104","type":"journal-article","created":{"date-parts":[[2004,11,20]],"date-time":"2004-11-20T02:47:43Z","timestamp":1100918863000},"page":"3104-3114","source":"Crossref","is-referenced-by-count":52,"title":["Infrequent cavity\u2010forming fluctuations in HPr from <i>Staphylococcus carnosus<\/i> revealed by pressure\u2010 and temperature\u2010dependent tyrosine ring flips"],"prefix":"10.1002","volume":"13","author":[{"given":"Mineyuki","family":"Hattori","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hua","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroaki","family":"Yamada","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuyuki","family":"Akasaka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfgang","family":"Hengstenberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfram","family":"Gronwald","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans Robert","family":"Kalbitzer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,1]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi010312u"},{"key":"e_1_2_7_3_1","first-page":"134","volume-title":"Nuclear magnetic resonance of biological macromolecules, Part A, Methods in enzymology","author":"Akasaka K.","year":"2001"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0301-4622(02)00018-2"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1090-7807(02)00179-9"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340170110"},{"key":"e_1_2_7_7_1","volume-title":"X\u2010PLOR version 3.1","author":"Br\u00fcnger A.T.","year":"1992"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1002\/bip.1979.360180206"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1098\/rspb.1975.0070"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(76)80734-X"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(75)80854-4"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bb.21.060192.001331"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1038\/nsb1101-932"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmre.1996.1033"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF03162178"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmre.1998.1614"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.pnmrs.2003.12.002"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00863707"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1038\/78963"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1063\/1.438208"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1110\/ps.9.4.693"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(81)80881-2"},{"key":"e_1_2_7_23_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(96)00157-8"},{"key":"e_1_2_7_24_1","doi-asserted-by":"publisher","DOI":"10.1016\/0263-7855(96)00009-4"},{"key":"e_1_2_7_25_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0031-8914(40)90098-2"},{"key":"e_1_2_7_26_1","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/6.4.417"},{"key":"e_1_2_7_27_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi972288j"},{"key":"e_1_2_7_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(99)77112-2"},{"key":"e_1_2_7_29_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja00381a009"},{"key":"e_1_2_7_30_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja00381a010"},{"key":"e_1_2_7_31_1","first-page":"55","article-title":"The mobile defect hypothesis of protein function","volume":"246","author":"Lumry R.","year":"1975","journal-title":"Coll. 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