Abstract：
:Proteins have many distinct tertiary folds (Richardson, J. S. (1981) Adv. Prot. Chem. 34, 167-339). The term tertiary fold refers to the spatial organization of secondary structure elements (alpha-helices and beta-strands). It is not known when, in the process of protein folding, a native tertiary fold emerges. Here, we show that the helical domain of human alpha-lactalbumin, in isolation, forms a molten globule with the same overall tertiary fold as that found in intact alpha-lactalbumin. Formation of this native-like fold does not require extensive, specific side-chain packing. Our results suggest that much of the information transfer from one-dimension to three-dimensions has occurred at the molten globule stage of protein folding.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Peng ZY,Kim PSdoi
10.1021/bi00174a021subject
Has Abstractpub_date
1994-03-01 00:00:00pages
2136-41issue
8eissn
0006-2960issn
1520-4995journal_volume
33pub_type
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