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Even though the protein does not exhibit reversible thermal unfolding, one can determine its stability parameters\u2014free energy, enthalpy, entropy, and melting temperature\u2014and also the distribution of stability throughout the protein, by using hydrogen exchange to measure the reversible cycling of the protein between native and unfolded states that occurs even under native conditions.<\/jats:p>","DOI":"10.1073\/pnas.94.21.11329","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:31:44Z","timestamp":1027693904000},"page":"11329-11332","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":85,"title":["Stability and dynamics in a hyperthermophilic protein with melting temperature close to\u2009200\u00b0C"],"prefix":"10.1073","volume":"94","author":[{"given":"Reuben","family":"Hiller","sequence":"first","affiliation":[{"name":"The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059; and Department of Biochemistry and Molecular Biology and the Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602"}]},{"given":"Zhi H.","family":"Zhou","sequence":"additional","affiliation":[{"name":"The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059; and Department of Biochemistry and Molecular Biology and the Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602"}]},{"given":"Michael W. 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