| LOCAL STRUCTURAL PREFERENCES IN THE ALPHA-LACTALBUMIN MOLTEN GLOBULE |
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| Author(s): PENG ZY, WU LC, KIM PS |
| Source: BIOCHEMISTRY Volume: 34 Issue: 10 Pages: 3248-3252 Published: MAR 14 1995 |
| Times Cited: 99 References: 45 |
| 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 nativelike 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. MIT, WHITEHEAD INST BIOMED RES, HOWARD HUGHES MED INST, DEPT BIOL, CAMBRIDGE, MA 02142 USA |
| Publisher: AMER CHEMICAL SOC, PO BOX 57136, WASHINGTON, DC 20037-0136 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: QM333 |
| ISSN: 0006-2960 |