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| THE FOLDING OF HEN LYSOZYME INVOLVES PARTIALLY STRUCTURED INTERMEDIATES AND MULTIPLE PATHWAYS |
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| Author(s): RADFORD SE, DOBSON CM, EVANS PA |
| Source: NATURE Volume: 358 Issue: 6384 Pages: 302-307 Published: JUL 23 1992 |
| Times Cited: 598 References: 45 |
| Abstract: Analysis of the folding of hen lysozyme shows that the protein does not become organized in a single cooperative event but that different parts of the structure become stabilized with very different kinetics. In particular, in most molecules the alpha-helical domain folds faster than the beta-sheet domain. Furthermore, different populations of molecules fold by kinetically distinct pathways. Thus, folding is not a simple sequential assembly process but involves parallel alternative pathways, some of which may involve substantial reorganization steps. |
| Document Type: Article |
| Language: English |
| Reprint Address: RADFORD, SE (reprint author), UNIV OXFORD, OXFORD CTR MOLEC SCI, S PARKS RD, OXFORD OX1 3QR, ENGLAND |
Addresses:
1. UNIV OXFORD, INORGAN CHEM LAB, OXFORD OX1 3QR, ENGLAND
2. UNIV CAMBRIDGE, CAMBRIDGE CTR MOLEC RECOGNIT, CAMBRIDGE CB2 1QW, ENGLAND
3. UNIV CAMBRIDGE, DEPT BIOCHEM, CAMBRIDGE CB2 1QW, ENGLAND |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: JE684 |
| ISSN: 0028-0836 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |