Myoglobin folding intermediate

Figure 5.7 Structural analysis of a 10ms folding intermediate of myoglobin using millisecond HX with a top-down workflow enabled by ECO fragmentation. Early development of structure is isolated to the C-terminus, particularly the C and H helices and is essentially absent from the N-terminus. Structured regions are indicated in dark gray. Reproduced with permission from Ref. [35]. 2010, American Chemical Society. (See insert for color representation of the figure.)...

D. A. Simmons and L. Konermann, Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospray mass spectrometry with on-hne isotope-pulse labeling. Biochemistry 42, 1906-1914 (2002). 

Simmons, D.A., Konermann, L. (2002) Characterization of Transient Protein Folding Intermediates during Myoglobin Reconstitution by Time-resolved Electrospray Mass Spectrometry with On-hne Isotopic Pulse Labeling. Biochemistry 41 1906-1914. 

In conclusion, the results on myoglobin analyzed here tk) not provide a test of the various aspects of the theory developed in Section VIII, mainly for lack of supplementary data. Certainly we do not note discrepanci between the behavior tlK model and experimental results, but our criteria as to what constitutes dkcrepancy are not very stringent Tlte theory presents a particular point of view, which in these cases does allow one to gain a re onable qualitative understanding of the experiments. The basic point in the theory k the instability of the intermediates in the folding process this is well reproduced by the lattice model, which allows one to calculate the kinetic behavior of a cooperative system with results which may, hopefully, be applied to other cooperative systems and in particular to protein molecules. Further experimental studies are needed to establish whether this is in fact the case. 

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