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Unfolding pathway of apomyoglobin. Simultaneous characterization of acidic conformational states by frequency domain fluorometry.

Abstract：

:The dynamic properties of the conformational states co-existing during the acid-induced unfolding of tuna apomyoglobin, a single tryptophan-containing protein, have been investigated simultaneously by frequency domain fluorometry. In the transition region, in the absence of salt, the tryptophanyl fluorescence emission arises from a bimodal lifetime distribution. The pH decrease causes a marked broadening of the short-lived distribution component whereas the other component, i.e. the long-lived one, remains unchanged and represented by a very narrow lifetime distribution whose width is similar to that of the native protein. The broadening of the short-lived distribution component observed on lowering the pH indicated that this component arises from fully unfolded molecules. This was further corroborated by acrylamide quenching studies at acidic pH. The collisional quenching rate constant of the short-lived distribution component, i.e. 8.9 x 10(9) M-1s-1, was found to be similar to that observed for a fully exposed residue. The long-lived distribution component was characterized by a lower collisional quenching rate constant, i.e. 2.3 x 10(9) M-1s-1. This value if compared to that determined for the native apoprotein at neutral pH, i.e. 4.0 x 10(8) M-1s-1, indicates that the native-like structure surviving the acid-induced transition possesses a large molecular flexibility.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Bismuto E,Irace G

doi

10.1006/jmbi.1994.1477

subject

Has Abstract

pub_date

1994-08-05 00:00:00

pages

103-9

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(84)71477-X

journal_volume

241

pub_type

杂志文章

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