Transition state in the folding of α‐lactalbumin probed by the 6‐120 disulfide bond

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1. 1Influence of an extrinsic crosslink on the folding pathway of ribonuclease A. Conformational and thermodynamic analysis of crosslinked (7-lysine, 41-lysine)-ribonuclease A1984 · 119 citations
2. 2Structure and stability of the molten globule state of guinea pig .alpha.-lactalbumin: A hydrogen exchange study1993 · 176 citations
3. 3Kinetics of disulfide bond reduction in .alpha.-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond1990 · 136 citations
4. 4Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds.1988 · 451 citations
5. 5Kinetic Consequences of the Removal of a Disulfide Bridge on the Folding of Hen Lysozyme1994 · 86 citations