Studies of beta-sheet structure in lysozyme by proton nuclear magnetic resonance. Assignments and analysis of spin-spin coupling constants.
Studies of beta-sheet structure in lysozyme by proton nuclear magnetic resonance. Assignments and analysis of spin-spin coupling constants.
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通过质子核磁共振研究溶菌酶中的β-折叠结构。
DOI：
10.1021/bi00262a036
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发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
Poulsen,FM
中科院分区：
文献类型：
--
作者：
Delepierre,M;Dobson,CM;Poulsen,FM
Muriel Delepierre、Christopher M. Dobson、**’* 和 Flemming M. Poulsen8 摘要：在 NMR 谱中，H ”、Hs 和 HN（酰胺）质子的共振已被指定为溶菌酶 3 片结构区域中的 10 个残基。这些指定主要是通过解释核奥弗豪瑟效应与自旋解耦相结合来实现的。发现参与主链氢键的 HN 氢可以交换尽管交换最慢的 HN 氢之一不被归类为涉及晶体结构中的氢键，但与 D20 溶剂的交换速度较慢。
Muriel Delepierre, Christopher M. Dobson,*’* and Flemming M. Poulsen8 abstract: Resonances of H “, Hs, and HN (amide) protons have been assigned in the NMR spectrum for ten residues in a region of/3-sheet structure of lysozyme. The assignments were achieved primarily by interpretation of nuclear Over-hauser effectsin conjunction with spin decoupling. The HN hydrogens involved in main-chain hydrogen bonding were found to exchange slowly with D20 solvent, although one of the most slowly exchanging HN hydrogens is not classified as being involvedin a hydrogen bond in the crystal structure.