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Partitioning the effects of changes in a protein to the folded or unfolded forms by using a thermodynamic cycle: a change in Escherichia coli thioredoxin does not affect the unfolded state.
Wynn R, Richards FM. Wynn R, et al. Biochemistry. 1993 Nov 30;32(47):12922-7. doi: 10.1021/bi00210a046. Biochemistry. 1993. PMID: 8251515
Previously, we have introduced a method whereby novel disulfide side chains can be produced in the interior of a protein by modifying a cysteine residue after denaturant-induced unfolding [Wynn, R., & Richards, F. M. (1993) Proteins: Struct., Funct., Genet. 2, 3 …
Previously, we have introduced a method whereby novel disulfide side chains can be produced in the interior of a protein by modifying a cyst …
Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry.
Ladbury JE, Kishore N, Hellinga HW, Wynn R, Sturtevant JM. Ladbury JE, et al. Among authors: wynn r. Biochemistry. 1994 Mar 29;33(12):3688-92. doi: 10.1021/bi00178a027. Biochemistry. 1994. PMID: 8142367
Data for the thermal denaturation of the reduced protein are presented, which on comparison to the data obtained for the oxidized form [Ladbury, J.E., Wynn, R., Hellinga, H.W., & Sturtevant, J.M. (1993) Biochemistry 32, 7526-7530] are used to establish thermodyn …
Data for the thermal denaturation of the reduced protein are presented, which on comparison to the data obtained for the oxidized form [Ladb …
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