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Characterizing Methyl-Bearing Side Chain Contacts and Dynamics Mediating Amyloid β Protofibril Interactions Using 13Cmethyl-DEST and Lifetime Line Broadening

机译：表征含甲基的侧链接触和动力学介导淀粉样β原纤维相互作用使用13 Cmethyl-DEST和终生线拓宽。

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Many details pertaining to the formation and interactions of protein aggregates associated with neurodegenerative diseases are invisible to conventional biophysical techniques. We recently introduced ¹⁵N dark-state exchange saturation transfer (DEST) and ¹⁵N lifetime line-broadening to study solution backbone dynamics and position-specific binding probabilities for amyloid β (Aβ) monomers in exchange with large (2–80 MDa) protofibrillar Aβ aggregates. Here we use ¹³Cmethyl DEST and lifetime line-broadening to probe the interactions and dynamics of methyl-bearing side chains in the Aβ-protofibril-bound state. We show that all methyl groups of Aβ40 populate direct-contact bound states with a very fast effective transverse relaxation rate, indicative of side-chain-mediated direct binding to the protofibril surface. The data are consistent with position-specific enhancements of

C_{methyl} - R_{2}^{tethered}

values in tethered states, providing further insights into the structural ensemble of the protofibril-bound state.

机译：关于与神经退行性疾病相关的蛋白质聚集体的形成和相互作用的许多细节是常规生物物理技术所看不见的。最近，我们引入了^{15 N暗态交换饱和转移（DEST）和^{15 N寿命延长线，以研究溶液骨架动力学和淀粉样蛋白β的位置特异性结合概率（ Aβ）单体与大量（2–80 MDa）原纤维Aβ聚集体交换。在这里，我们使用^{13 C甲基DEST和延长寿命的线来研究处于Aβ-原纤维结合状态的含甲基侧链的相互作用和动力学。我们显示，Aβ40的所有甲基基团以非常快速的有效横向弛豫速率构成直接接触结合状态，表明侧链介导的直接结合至原纤维表面。数据与 $C$}}}

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期刊名称 other
作者
Dr. Nicolas L. Fawzi; Dr. David S. Libich; Dr. Jinfa Ying; Dr. Vitali Tugarinov; Dr. G. Marius Clore;
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作者单位

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年(卷),期 -1(53),39
年度 -1
页码 10345–10349
总页数 11
原文格式 PDF
正文语种
中图分类
关键词
amyloid β high-molecular-weight assemblies NMR spectroscopy protein–protein interactions;

机译：淀粉样蛋白β;高分子量组装体;NMR光谱;蛋白质间相互作用;

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专利

1. Characterizing Methyl-Bearing Side Chain Contacts and Dynamics Mediating Amyloid β Protofibril Interactions Using ~(13)C_(methyl)-DEST and Lifetime Line Broadening [J] . Nicolas L. Fawzi, David S. Libich, Jinfa Ying Angewandte Chemie . 2014,第39期

机译：使用〜（13）C_（甲基）-DEST和终生线拓宽表征含甲基的侧链接触和介导淀粉样β原纤维相互作用的动力学
2. Polyproline chains destabilize the Alzheimer's amyloid-beta protofibrils: A molecular dynamics simulation study [J] . Kanchi Pavan Krishna, Dasmahapatra Ashok Kumar Journal of molecular graphics & modelling . 2019,第期

机译：聚丙烯链破坏了阿尔茨海默蛋白淀粉样蛋白酶β原纤维：分子动力学模拟研究
3. Interactions of a Water-Soluble Fullerene Derivative with Amyloid-β Protofibrils: Dynamics, Binding Mechanism, and the Resulting Salt-Bridge Disruption [J] . Xiaoying Zhou, Wenhui Xi, Yin Luo The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical . 2014,第24期

机译：水溶性富勒烯衍生物与淀粉样β原纤维的相互作用：动力学，绑定机制和导致的盐桥破坏。
4. Molecular dynamics study on the effect of lipid membrane mechanical properties on the interaction between β-amyloid and lipid membrane [C] . Yulin Ji, Yujuan Wang, Wei Si, International Conference on Signal Processing and Communication Systems . 2020

机译：脂膜力学性能对β-淀粉样膜与脂质膜相互作用影响的分子动力学研究
5. Interprotomer contacts in actin filament and its dynamics, interactions and function [D] . Durer, Zeynep Aslihan 2011

机译：肌动蛋白丝中的启动子间接触及其动力学，相互作用和功能
6. Atomic-resolution map of the interactions between an amyloid inhibitor protein and amyloid β (Aβ) peptides in the monomer and protofibril states [O] . Moustafa Algamal, Rashik Ahmed, Naeimeh Jafari, 2017

机译：单体状态和原纤维状态中淀粉样蛋白抑制剂蛋白与淀粉样蛋白β（Aβ）肽之间相互作用的原子分辨率图
7. Differences in Dynamics and Stability of the Wild Type Beta-Amyloid Aβ1-40, and ΔE22-Aβ1-39 (Japanese) Mutant Protofibril Structures, a Molecular Dynamics Study [O] . Johnson Kipp W., Sosnick Tobin R., Freed Karl F., 2014

机译：分子动力学研究，野生型β-淀粉样蛋白Aβ1-40和ΔE22-Aβ1-39（日本）突变原纤维结构的动力学和稳定性差异

Characterizing Methyl-Bearing Side Chain Contacts and Dynamics Mediating Amyloid β Protofibril Interactions Using 13Cmethyl-DEST and Lifetime Line Broadening

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