REVERSIBLE UNFOLDING OF AN ISOLATED HEPARIN AND DNA-BINDING FRAGMENT, THE 1ST TYPE-III MODULE FROM FIBRONECTIN
REVERSIBLE UNFOLDING OF AN ISOLATED HEPARIN AND DNA-BINDING FRAGMENT, THE 1ST TYPE-III MODULE FROM FIBRONECTIN
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DOI：
10.1016/0167-4838(92)90234-5
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发表时间：
1992-02-13
期刊：
影响因子：
--
通讯作者：
INGHAM, KC
中科院分区：
文献类型：
--
作者：
LITVINOVICH, SV;NOVOKHATNY, VV;INGHAM, KC
Several fragments containing all or part of the first type III homology unit of fibronectin were isolated and their folding properties examined by fluorescence spectroscopy and differential scanning calorimetry. Each fragment exhibits a reversible unfolding transition when heated or titrated with guanidinium chloride. This indicates that an isolated type III module can fold independently in the absence of neighboring modules. A comparison of the specific enthalpies of unfolding of these fragments with those of well-studied globular proteins suggests that this type III unit is composed of a stable core flanked by less compact or unstructured regions. Comparison of the heparin-binding properties of these fragments revealed that removal of 12 amino acids from the amino terminus of the largest one (Ile-585 to Val-675) increased its affinity for immobilized heparin such that it now binds at physiological ionic strength.
