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Prosequence-Mediated Disulfide Coupled Folding of the Peptide Hormones Guanylin and Uroguanylin

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In contrast to their prohormones the mature peptide hormones guanylin and uroguanylin are not able to fold to their native disulfide connectivities upon oxidative folding. Structural properties of both peptide hormones and their precursor proteins as well as the role of their prosequences in proper disulfide coupled folding are reviewed. In addition, the structural behavior of a proguanylin mutant that closely resembles prouroguanylin has been investigated to gain further insight into structural properties of this homologous precursor protein.

Keywords: disulfide bonds; folding; guanylin; peptide hormone; proguanylin; prosequence; prouroguanylin; uroguanylin

Document Type: Review Article


Affiliations: Lehrstuhl fur Biopolymere, Universitat Bayreuth, Universitatstra├če 30, 95447 Bayreuth, Germany.

Publication date: February 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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