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MEASUREMENT OF THE BETA-SHEET-FORMING PROPENSITIES OF AMINO-ACIDS
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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