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• W2081531609 startingPage "3248" @default.
• W2081531609 abstract "Molten globules have been proposed to be general intermediates in protein folding. Despite numerous studies, a detailed description of the structure of a molten globule remains elusive. Recently, we showed that the molten globule formed by the helical domain of alpha-lactalbumin (alpha-LA) has a native-like backbone topology. Here we probe local structural preferences in the helical domain of the alpha-LA molten globule by analyzing a set of native and nonnative single disulfide bond variants using a combination of circular dichroism spectroscopy and determination of the equilibrium constant for disulfide bond formation. We find that the region surrounding the 28-111 disulfide bond has a high preference to adopt a native-like structure. Formation of other native or nonnative disulfide bonds is significantly less favorable. Our results suggest that molten globules contain regions with varying degrees of specificity for native-like structure and that the core region surrounding the 28-111 disulfide bond plays an important role in alpha-LA folding by stabilizing the molten globule intermediate." @default.
• W2081531609 created "2016-06-24" @default.
• W2081531609 creator A5035781067 @default.
• W2081531609 creator A5066675626 @default.
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• W2081531609 date "1995-03-01" @default.
• W2081531609 modified "2023-09-26" @default.
• W2081531609 title "Local Structural Preferences in the .alpha.-Lactalbumin Molten Globule" @default.
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• W2081531609 doi "https://doi.org/10.1021/bi00010a014" @default.
• W2081531609 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7880819" @default.
• W2081531609 hasPublicationYear "1995" @default.
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