Information de reference pour ce titreAccession Number: | 00008400-200634020-00002.
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Author: | Siemer, Ansgar B. a; Ritter, Christiane b; Steinmetz, Michel O. c; Ernst, Matthias a; Riek, Roland b; Meier, Beat H. a,*
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Institution: | (a)Physical Chemistry, ETH Zurich, CH-8093, Zurich, Switzerland. (b)Structural Biology Laboratory, The Salk Institute, La Jolla, CA, 92037, USA. (c)Biomolecular Research, Structural Biology, Paul Scherrer Institut, CH-5232, Villigen, PSI, Switzerland.
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Title: | 13C, 15N Resonance assignment of parts of the HET-s prion protein in its amyloid form.[Article]
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Source: | Journal of Biomolecular NMR. 34(2):75-87, February 2006.
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Abstract: | The partial 15N and 13C solid-state NMR resonance assignment of the HET-s prion protein fragment 218-289 in its amyloid form is presented. It is based on experiments measured at MAS frequencies in the range of 20-40 kHz using exclusively adiabatic polarization-transfer schemes. The resonance assignment within each residue is based on two-dimensional 13C[double bond]13C correlation spectra utilizing the DREAM mixing scheme. The sequential linking of the assigned residues used a set of two- and three-dimensional 15N[double bond]13C correlation experiments. Almost all cross peaks visible in the spectra are assigned, but only resonances from 43 of the 78 amino-acid residues could be detected. The missing residues are thought to be highly disordered and/or highly dynamic giving rise to broad resonance lines that escaped detection in the experiments applied. The line widths of the observed resonances are narrow and comparable to line widths observed in micro-crystalline samples. The 43 assigned residues are located in two fragments of about 20 residues.
(C)2006 Kluwer Academic Publishers
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Author Keywords: | amyloid; HET-s; prions; solid-state NMR.
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Language: | English.
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Document Type: | Article: PDF Only.
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Journal Subset: | Life Sciences.
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ISSN: | 0925-2738
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NLM Journal Code: | bjm, 9110829
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