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Quench‐flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate
Author(s) -
Tsui Vickie,
Garcia Carlos,
Cavagnero Silvia,
Siuzdak Gary,
Dyson H. Jane,
Wright Peter E.
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.1.45
Subject(s) - chemistry , mass spectrometry , folding (dsp implementation) , electrospray ionization , protein folding , mass spectrum , crystallography , analytical chemistry (journal) , chromatography , biochemistry , electrical engineering , engineering
Folding of apomyoglobin is characterized by formation of a compact intermediate that contains substantial helicity. To determine whether this intermediate is obligatory or whether the protein can fold directly into the native state via an alternate parallel pathway, we have combined quench‐flow hydrogen‐exchange pulse labeling techniques with electrospray ionization mass spectrometry. The mass spectra of apomyoglobin obtained at various refolding times suggest that apomyoglobin indeed folds through a single pathway containing an obligatory intermediate with a significant hydrogen‐bonded secondary structure content.