Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate

Author:

Tsui Vickie,Garcia Carlos,Cavagnero Silvia,Siuzdak Gary,Dyson H. Jane,Wright Peter E.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference18 articles.

1. Spin glasses and the statistical mechanics of protein folding;Bryngelson;Proc Natl Acad Sci USA,1987

2. Cavagnero S Dyson HJ Wright PE 1998 Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin J Mol Biol.

3. Structural and dynamic characterization of partially folded states of myoglobin and implications for protein folding;Eliezer;Nature Struct Biol,1998

4. Structural characterization of a partly folded apomyoglobin intermediate;Hughson;Science,1990

5. Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin;Jamin;Nature Struct Biol,1996

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