Abstract：
:Three unfolding domains in rabbit muscle aldolase destabilized in 3 M urea have been identified from their unfolding rate constants (0.10, 0.036, and 0.0064 min-1). The populations of folded and various, partially unfolded forms were determined by amide hydrogen exchange and mass spectrometry. Results of this study show that unfolding domains may include multiple, noncontiguous segments of the backbone and that different regions of helices may belong to different unfolding domains. In addition, these results show that the domain unfolding most rapidly is located distant from the subunit binding surfaces and has the greatest access to the denaturant. The bimodal intermolecular distributions of deuterium found in this study show that unfolding of these domains is cooperative. It is proposed that these unfolding domains are correlated with local energy minima in the free-energy folding surface of aldolase. In addition to the three unfolding domains, there are three short segments that do not unfold in 3 M urea. These segments, which are located in the subunit binding surface, identify the most stable regions of aldolase. This study also demonstrates that it is now possible to identify and characterize unfolding domains in relatively large (Mr 158 000) proteins.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Deng Y,Smith DLdoi
10.1021/bi972711osubject
Has Abstractpub_date
1998-05-05 00:00:00pages
6256-62issue
18eissn
0006-2960issn
1520-4995pii
bi972711ojournal_volume
37pub_type
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