NDLI: Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.

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Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jaroniec, Christopher P. Astrof, Nathan S. Griffin, Robert G. Macphee, Cait E. Dobson, Christopher M.
Description	Author Affiliation: Jaroniec CP ( Department of Chemistry and Center for Magnetic Resonance, Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.);
Abstract	The molecular conformation of peptide fragment 105-115 of transthyretin, TTR(105-115), previously shown to form amyloid fibrils in vitro, has been determined by magic-angle spinning solid-state NMR spectroscopy. 13C and 15N linewidth measurements indicate that TTR(105-115) forms a highly ordered structure with each amino acid in a unique environment. 2D 13C-13C and 15N-13C-13C chemical shift correlation experiments, performed on three fibril samples uniformly 13C,15N-labeled in consecutive stretches of 4 aa, allowed the complete sequence-specific backbone and side-chain 13C and 15N resonance assignments to be obtained for residues 105-114. Analysis of the 15N, 13CO, 13Calpha, and 13Cbeta chemical shifts allowed quantitative predictions to be made for the backbone torsion angles phi and psi. Furthermore, four backbone 13C-15N distances were determined in two selectively 13C,15N-labeled fibril samples by using rotational-echo double-resonance NMR. The results show that TTR(105-115) adopts an extended beta-strand conformation that is similar to that found in the native protein except for substantial differences in the vicinity of the proline residue.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	26
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Chemistry Peptide Fragments Prealbumin Amino Acid Sequence Microscopy, Electron Nuclear Magnetic Resonance, Biomolecular Protein Conformation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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