Thread: NMR paper NMR analysis of staphylococcal nuclease thermal quench refolding kinetics.
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Default NMR analysis of staphylococcal nuclease thermal quench refolding kinetics.
NMR analysis of staphylococcal nuclease thermal quench refolding kinetics.

Related Articles NMR analysis of staphylococcal nuclease thermal quench refolding kinetics.

Protein Sci. 1993 May;2(5):851-8

Authors: Kautz RA, Fox RO

Thermally unfolded staphylococcal nuclease has been rapidly quenched to temperatures near 0 degree C and the refolding behavior examined using an NMR kinetic experiment. Unfolded protein, exhibiting random coil chemical shifts, persists following the quench and refolds in two distinct kinetic phases. A protein folding intermediate with a trans Lys 116-Pro 117 peptide bond is transiently overpopulated and relaxes to the predominantly cis native cis-trans equilibrium. The rate of trans-->cis isomerization in the native-like nuclease intermediate is approximately 100-fold faster than that observed in a Lys-Pro model peptide. The activation enthalpy of 20 kcal/mol observed for the nuclease Lys 116-Pro 117 peptide bond is comparable to that observed for other X-Pro isomerizations.

PMID: 8495202 [PubMed - indexed for MEDLINE]



Source: PubMed
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