通过15N-1H NMR光谱获得的抹香鲸肌红蛋白的酰胺质子氢交换率。
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.
作者信息
Cavagnero S, Thériault Y, Narula S S, Dyson H J, Wright P E
机构信息
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
出版信息
Protein Sci. 2000 Jan;9(1):186-93. doi: 10.1110/ps.9.1.186.
Abstract
The hydrogen exchange behavior of exchangeable protons in proteins can provide important information for understanding the principles of protein structure and function. The positions and exchange rates of the slowly-exchanging amide protons in sperm whale myoglobin have been mapped using 15N-1H NMR spectroscopy. The slowest-exchanging amide protons are those that are hydrogen bonded in the longest helices, including members of the B, E, and H helices. Significant protection factors were observed also in the A, C, and G helices, and for a few residues in the D and F helices. Knowledge of the identity of slowly-exchanging amide protons forms the basis for the extensive quench-flow kinetic folding experiments that have been performed for myoglobin, and gives insights into the tertiary interactions and dynamics in the protein.
摘要
蛋白质中可交换质子的氢交换行为可为理解蛋白质结构和功能原理提供重要信息。利用15N-1H核磁共振光谱法已绘制出抹香鲸肌红蛋白中缓慢交换酰胺质子的位置和交换速率。交换最慢的酰胺质子是那些在最长螺旋中形成氢键的质子，包括B、E和H螺旋的成员。在A、C和G螺旋中也观察到了显著的保护因子，以及D和F螺旋中的少数残基。了解缓慢交换酰胺质子的身份构成了对肌红蛋白进行广泛的淬灭流动动力学折叠实验的基础，并有助于深入了解蛋白质中的三级相互作用和动力学。
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