Work

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

Year: 1999

Type: article

Abstract: 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.

Source: Protein Science

DOI: 10.1110/ps.8.1.45

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

Institution: Scripps Research Institute

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: G1609798843, G4780582393, DIOXYGEN-COPPER COMPLEXES: PROPERTIES AND REACTIVITY, NMR Studies of Chaperone-Client Protein Interactions