Native conformational tendencies in unfolded polypeptides: Development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins

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[1] Native conformational tendencies in unfolded polypeptides: Development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins
Narayan, M
Welker, E
Scheraga, HA
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (08) : 2036 - 2037
[2] Multiple Disulfide-Bonded States of Native Proteins: Estimate of Number Using Probabilities of Disulfide Bond Formation
Hogg, Philip J.
MOLECULES, 2020, 25 (23):
[3] Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: Implications for the mechanism of oxidative folding of RNase A
English, BP
Welker, E
Narayan, M
Scheraga, HA
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (18) : 4995 - 4999