Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils

被引：26
作者：
Bauer, Thomas [1 ]
Dotta, Claudio [1 ]
Balacescu, Livia [1 ]
Gath, Julia [1 ]
Hunkeler, Andreas [1 ]
Bockmann, Anja [2 ]
Meier, Beat H. [1 ]
机构：
[1] Swiss Fed Inst Technol, Phys Chem, Vladimir Prelog Weg 2, CH-8093 Zurich, Switzerland
[2] Univ Lyon 1, CNRS, UMR 5086, Inst Biol & Chim Prot, 7 Passage Vercors, F-69367 Lyon, France
来源：
JOURNAL OF BIOMOLECULAR NMR | 2017年 / 67卷 / 01期
基金：
瑞士国家科学基金会;
关键词：
Solid-state NMR; Low-temperature; Line broadening; Fibrils; Protein; HET-s; DYNAMIC NUCLEAR-POLARIZATION; HET-S PRION; HET-S(218-289) AMYLOID FIBRILS; ATOMIC-RESOLUTION STRUCTURE; ANTIFREEZE PROTEIN; PODOSPORA-ANSERINA; MAS NMR; SPECTROSCOPY; SCHEME; ICE;
D O I：
10.1007/s10858-016-0083-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The temperature-dependent resonance-line broadening of HET-s(218-289) in its amyloid form is investigated in the range between 110 K and 280 K. Significant differences are observed between residues in the structured hydrophobic triangular core, which are broadened the least and can be detected down to 100 K, and in the solvent-exposed parts, which are broadened the most and often disappear from the observed spectrum around 200 K. Below the freezing of the bulk water, around 273 K, the protein fibrils are still surrounded by a layer of mobile water whose thickness decreases with temperature, leading to drying out of the fibrils.
引用
收藏
页码：51 / 61
页数：11
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