Premium
Spectroscopic and thermodynamic evidence for a complex denaturation mechanism of bovine β‐lactoglobulin A
Author(s) -
GarcíaHernández Enrique,
HernándezArana Andrés,
Zubillaga Rafael A.,
RojoDomínguez Arturo
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203172
Subject(s) - denaturation (fissile materials) , chemistry , native state , crystallography , lipocalin , molecule , protein structure , biochemistry , organic chemistry , nuclear chemistry
We present a spectroscopic and calorimetric study on the thermal denaturation of bovine β‐lactoglobulin (β‐lg) variant A. Spectroscopic data allowed detection of a stable intermediate emerging from structural modifications restricted to local regions of the native molecule. It is suggested that this kind of intermediate could be a common property of lipocalins. Using the same set of parameters that has successfully related thermodynamics and structural properties of other proteins, it is shown that the thermally denatured state of β‐lg retains a significant amount of buried hydrophobic surface area. Thus, despite being a small protein composed of a single structural domain, β‐lg exhibits a complex unfolding mechanism, comprising at least two other species different from the native and completely unfolded states.