Elsevier

Surface Science

Volume 284, Issues 1–2, 10 March 1993, Pages L411-L415
Surface Science

Surface science letters
Direct observation of the secondary structure of unfolded pseudomonas-cytochrome c551 by scanning tunneling microscopy

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Abstract

The denaturation of pseudomonas-cytochrome c551 at the air-water interface was studied using scanning tunneling microscopy (STM). The STM images indicate that the native secondary and tertiary structures of this protein has been virtually lost at such interface. The polypeptide chains of the unfolded protein are nearly fully extended, and highly aggregated in a localized region, forming a crystalline or a twisted rope-like structure. Our observation demonstrates the capability of STM in studying the unfolding of proteins, and also suggests the possibility of using STM to directly sequence the amino acid residues of a protein.

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