Probing the structure of folding intermediates
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Cited by (91)
Stochastic strategy to analyze protein folding
2005, Physica A: Statistical Mechanics and its ApplicationsReversible denaturation of the soybean Kunitz trypsin inhibitor
2003, Archives of Biochemistry and BiophysicsCitation Excerpt :The increase in fluorescence intensity did approximate a two-state system with a midpoint at approximately 65 °C. As expected, upon cooling of the sample, the fluorescence intensity from added ANS decreased, indicating a compaction of the protein consistent with a “hydrophobic collapse” leading to the native form [28]. The CD data provide strong evidence that indicate global unfolding in SKTI during thermal denaturation.
Unfolded state of peptides
2002, Advances in Protein ChemistryNew stochastic strategy to analyze helix folding
2002, Biophysical JournalCitation Excerpt :The allowed values for the pairs of dihedral angles about the Cα atoms, which are limited by steric constraints, were determined by Ramachandran et al. (1963) and are summarized in the so-called Ramachandran map. Important advances are found in the theoretical field of chain topologies prediction (Rooman et al., 1991) and also regarding the folding patterns determined by experimental studies (Richards, 1991; Dobson, 1992; Elöve et al., 1992; Haynie and Freire, 1993; Kiefhaber et al., 1992; Radford et al., 1992; Khorazanizadeh et al., 1993; Evans and Radford, 1994; Clarke et al., 1999) as well as by theoretical ones (Dill, 1990, 1993; Shakhnovich, 1994; Sali et al., 1994; Wolynes et al., 1995; Bryngelson et al., 1995; Pande et al., 1998; Hiltpold et al., 2000). Helices are the most prevalent secondary structural motif observed in proteins with known structure.