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Science 13 August 1993:
Vol. 261. no. 5123, pp. 879 - 885
DOI: 10.1126/science.8346440
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Articles
Science, Vol 261, Issue 5123, 879-885
Copyright © 1993 by American Association for the Advancement of Science
Metal ion-dependent modulation of the dynamics of a designed protein
TM Handel,
SA Williams,
and
WF DeGrado
Du Pont Merck Pharmaceutical Company, Wilmington, DE 19880-0328.
The peptide alpha 4 is a designed four-helix bundle that contains a highly simplified hydrophobic core composed exclusively of leucine residues; its tertiary structure is therefore largely dictated by hydrophobic forces. This small protein adopts a structure with properties intermediate between those of the native and molten globule states of proteins: it is compact, globular, and has very stable helices, but its apolar side chains are mobile and not as well packed as in many natural proteins. To induce a more native-like state, two Zn(2+)-binding sites were introduced into the protein, thereby replacing some of the non-specific hydrophobic interactions with more geometrically restrictive metal-ligand interactions. In the metal-bound state, this protein has properties that approach those of native proteins. Thus, hydrophobic interactions alone are sufficient to drive polypeptide chain folding nearly to completion, but specific interactions are required for a unique structure.
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