title: Dynamics and thermodynamics of hyperthermophilic proteins by hydrogen exchange.
abstract: The naturally occurring hydrogen exchange of protein molecules can provide nonperturbing site-resolved measurements of protein stability and flexibility and changes therein. The measurement and understanding of these issues is especially pertinent to studies of thermophilic proteins. This chapter briefly reviews the considerations necessary for measuring hydrogen exchange and translating HX measurements into these detailed protein parameters.
authors.affiliation: Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19109-6059, USA.
authors.forename: S W
authors.initials: SW
authors.lastname: Englander
authors.forename: R
authors.initials: R
authors.lastname: Hiller
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry*; D008956:Models, Chemical; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D019843:Archaeal Proteins; D006859:Hydrogen