Diethyl pyrocarbonate inactivates swine pepsinogen by reaction at amino groups

McPhie, Peter; Chiu, Fang-Ting

doi:10.1016/0003-9861(81)90479-3

Cited by 2 publications

(1 citation statement)

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“…Rosa & Richards (1979)]. In contrast, previous chemical modification studies on pepsinogen demonstrated increased reactivity to diethyl pyrocarbonate in the amino-terminal region, while the protein was undergoing the Is -N reaction (McPhie & Chiu, 1981). As this region becomes protected in a late step in folding, it may stabilize the zymogen by acting as a "key stone" rather than a nucleus.…”

Section: Discussionmentioning

confidence: 98%

Swine pepsinogen folding intermediates are highly structured, motile molecules

McPhie¹

1982

Biochemistry

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Refolding of urea- or alkali-unfolded swine pepsinogen occurs by rapid formation of partially folded intermediates (Is) which are slowly converted into the native protein (N). This slow reaction involves isomerization of proline residues in the protein to the configurations occurring in N. Kinetic studies on changes in absorbance or circular dichroism indicate Is to be close to the native structure, which fluorescence and hydrogen exchange measurements show Is to be much more open to solvent than N. Fluorescent probe binding suggests that Is has a more hydrophobic surface than N. These contrasting results are interpreted to show that the presence of wrong proline residues does not greatly inhibit the overall folding of pepsinogen but prevents close packing of structural elements into the highly cooperative, stable, native form. Is may be very similar to N in average structure, but is a much more fluctuating species.

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Section: Discussionmentioning

confidence: 98%