Microsecond folding dynamics of apomyoglobin at acidic pH.

@article{Xu2012MicrosecondFD,
  title={Microsecond folding dynamics of apomyoglobin at acidic pH.},
  author={Ming Xu and Olga Beresneva and Ryan R. Rosario and Heinrich Roder},
  journal={The journal of physical chemistry. B},
  year={2012},
  volume={116 23},
  pages={7014-25}
}
Apomyolgobin (apoMb) is an important model for understanding the folding mechanism of helical proteins. This study focuses on a partially structured state of sperm whale apoMb populated at pH 4.2 (M-state), which structurally resembles a late kinetic intermediate in the formation of the native state (N) at higher pH. The thermodynamics and cooperativity of apoMb folding at pH 4.2 and 6.2 were studied by global analysis of the urea-induced unfolding transitions monitored by tryptophan… CONTINUE READING

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