Dead time pulse labeling HDX NMR None proton occupancy < 0.6 MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL

Dead-time pulse-labeling experiment, in which the unfolded protein sample in D2O and 8.5 M D-urea was mixed with a H2O solution at pH 10.2 by a ratio of 1:9. After 13 ms, the sample was quenched at pH 3.0. At pH 10.2 and 25 °C, unprotected amide deuterons can exchange with solvent protons in less than 1 ms.

Dead time pulse labeling HDX NMR None 0.6 < proton occupancy < 0.8 MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL

Dead-time pulse-labeling experiment, in which the unfolded protein sample in D2O and 8.5 M D-urea was mixed with a H2O solution at pH 10.2 by a ratio of 1:9. After 13 ms, the sample was quenched at pH 3.0. At pH 10.2 and 25 °C, unprotected amide deuterons can exchange with solvent protons in less than 1 ms.

Native exchange NMR None ΔG(op)(kcal/mol) > 15 MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL

The exchange of 114 of the 164 backbone amide protons in T4 lysozyme was monitored as a function of denaturant concentration (eleven samples between 0 M and 2 M GdmCl). Exchange was initiated by spinning the samples through a Quick-sep spin column packed with G-25 resin pre-equilibrated in deuterated buffer (50 mM sodium phosphate, pD 6.0, 0.1 M KCl) with varying amounts of per-deuterated GdmCl. All of these denaturant concentrations are below the folding transition measured by global probes. Exchange was measured by two-dimensional 1H-15N HSQC spectra taken over a period of hours to months.

Native exchange NMR None 13 < ΔG(op)(kcal/mol) < 15 MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL

The exchange of 114 of the 164 backbone amide protons in T4 lysozyme was monitored as a function of denaturant concentration (eleven samples between 0 M and 2 M GdmCl). Exchange was initiated by spinning the samples through a Quick-sep spin column packed with G-25 resin pre-equilibrated in deuterated buffer (50 mM sodium phosphate, pD 6.0, 0.1 M KCl) with varying amounts of per-deuterated GdmCl. All of these denaturant concentrations are below the folding transition measured by global probes. Exchange was measured by two-dimensional 1H-15N HSQC spectra taken over a period of hours to months.

Native exchange NMR None 11 < ΔG(op)(kcal/mol) < 13 MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL

The exchange of 114 of the 164 backbone amide protons in T4 lysozyme was monitored as a function of denaturant concentration (eleven samples between 0 M and 2 M GdmCl). Exchange was initiated by spinning the samples through a Quick-sep spin column packed with G-25 resin pre-equilibrated in deuterated buffer (50 mM sodium phosphate, pD 6.0, 0.1 M KCl) with varying amounts of per-deuterated GdmCl. All of these denaturant concentrations are below the folding transition measured by global probes. Exchange was measured by two-dimensional 1H-15N HSQC spectra taken over a period of hours to months.