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| MEASUREMENT OF THE BETA-SHEET-FORMING PROPENSITIES OF AMINO-ACIDS |
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| Author(s): MINOR DL, KIM PS |
| Source: NATURE Volume: 367 Issue: 6464 Pages: 660-663 Published: FEB 17 1994 |
| Times Cited: 355 References: 29 |
| Abstract: SEVERAL model systems have been used to evaluate the alpha-helical propensities of different amino acids(1-7). In contrast, experimental quantitation of beta-sheet preferences has been addressed in only one model system, a zinc-finger peptide(8). Here we measure the relative propensity for beta-sheet formation of the twenty naturally occurring amino acids in a variant of the small, monomeric, beta-sheet-rich, IgG-binding domain from protein G. Amino-acid substitutions were made at a guest site on the solvent-exposed surface of the beta-sheet. Several criteria were used to establish that the mutations did not cause significant structural changes: binding to the Fc domain of IgG, calorimetric unfolding and NMR spectroscopy. Characterization of the thermal stabilities of these proteins leads to a thermodynamic scale for beta-sheet propensities that spans a range of similar to 2 kcal mol(-1) for the naturally occurring amino acids, excluding proline. The magnitude of the differences suggests that beta-sheet preferences can be important determinants of protein stability. |
| Document Type: Article |
| Language: English |
| Reprint Address: MINOR, DL (reprint author), MIT, HOWARD HUGHES MED INST, WHITEHEAD INST BIOMED RES, DEPT CHEM, 9 CAMBRIDGE CTR, CAMBRIDGE, MA 02142 USA |
Addresses:
1. MIT, HOWARD HUGHES MED INST, WHITEHEAD INST BIOMED RES, DEPT BIOL, CAMBRIDGE, MA 02142 USA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: MW688 |
| ISSN: 0028-0836 |
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