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This study assembled a set of 91 natively unfolded proteins (i.e., IDPs with extended disorder, such as native coils and native pre-molten globules), which at physiological conditions have been reported to have the NMR chemical shifts of a random-coil, and/or lack significant ordered secondary structure (as determined by CD or FTIR), and/or show hydrodynamic dimensions close to those typical of an unfolded polypeptide chain (Uversky et al., 2000a)

Technical Specifications Applications / Use Cases This compound is strictly utilized in non-clinical, controlled environments

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118 Redox reactions at key cysteine residuesnamely, s -glutathionylation at Cys346 119 and reduction of the Cys272-X-X-Cys275 disulphidealso enhance CBS enzymatic activity