NDLI: De novo design of a monomeric three-stranded antiparallel beta-sheet.

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De novo design of a monomeric three-stranded antiparallel beta-sheet.

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De novo design of a monomeric three-stranded antiparallel beta-sheet.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jiménez, M. A. Santoro, J. de Alba, E. Rico, M.
Description	Country affiliation: Spain Author Affiliation: de Alba E ( Instituto de Estructura de la Materia, Consejo Superior de Investigaciones Científicas, Madrid, Spain.)
Abstract	Here we describe the NMR conformational study of a 20-residue linear peptide designed to fold into a monomeric three-stranded antiparallel beta-sheet in aqueous solution. Experimental and statistical data on amino acid beta-turn and beta-sheet propensities, cross-strand side-chain interactions, solubility criteria, and our previous experience with beta-hairpins were considered for a rational selection of the peptide sequence. Sedimentation equilibrium measurements and NMR dilution experiments provide evidence that the peptide is monomeric. Analysis of 1H and 13C-NMR parameters of the peptide, in particular NOEs and chemical shifts, and comparison with data obtained for two 12-residue peptides encompassing the N- and C-segments of the designed sequence indicates that the 20-residue peptide folds into the expected conformation. Assuming a two-state model, the exchange kinetics between the beta-sheet and the unfolded peptide molecules is in a suitable range to estimate the folding rate on the basis of the NMR linewidths of several resonances. The time constant for the coil-beta-sheet transition is of the order of several microseconds in the designed peptide. Future designs based on this peptide system are expected to contribute greatly to our knowledge of the many factors involved in beta-sheet formation and stability.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	4
Volume Number	8
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1999-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Models, Chemical Protein Folding Protein Structure, Secondary Amino Acids Chemistry Magnetic Resonance Spectroscopy Models, Molecular Peptide Biosynthesis Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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