相关实验视频
Updated: Jul 4, 2025

12:42
Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
15.1K
在微秒时间尺度折叠小蛋白质后,对毫秒时间尺度结构进化的实验证据
C Blake Wilson1, Wai-Ming Yau1, Robert Tycko1
1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
Physical review letters
|February 9, 2024
概括
小蛋白快速折叠,但维林头饰子域 (HP35) 需要缓慢回火才能完全折叠. 时间解析的固态NMR揭示了发生在毫秒的侧链重排.
科学领域:
- 生物物理学的生物物理.
- 蛋白质动力学 蛋白质动力学
- 结构生物学是结构生物学.
背景情况:
- 众所周知,小蛋白质可以在微秒内折叠.
- 维林头饰子域 (HP35) 的折叠过程在原子层面还没有得到充分的描述.
研究的目的:
- 为了研究35个残留维林头饰子域 (HP35) 的折叠动力学.
- 为了识别HP35折叠中涉及的任何以前未被检测到的缓慢过程.
主要方法:
- 使用时间分辨率固态核磁共振 (ssNMR) 光谱.
- 在快速冷却后和快速冷之前,在30°C处冷的HP35溶液中获得13C ssNMR光谱.
- 采用一个可变的实验时间 (τe) 来捕捉动态变化.
主要成果:
- 证明HP35的完全折叠需要缓慢的回火过程.
- 在3-10毫秒的时间尺度上观察到光谱变化.
- 将这些变化归因于在化阶段蛋白质侧链的缓慢重新排列.
结论:
- 折叠HP35不仅是一个快速的过程.
- 一个缓慢的火机制,涉及毫秒时间尺度的侧链动态,对于完整的HP35折叠至关重要.
- 时间解析的ssNMR在检测缓慢的蛋白质动态方面是有效的.
更多相关视频
相关概念视频
Protein Folding
118.1K
Overview
118.1K
Molecular Chaperones and Protein Folding
18.0K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
18.0K
Protein Dynamics in Living Cells
2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K
Protein Organization
137.8K
Overview
137.8K

