通过碳-13核磁共振光谱法检测溶菌酶中新型温度依赖性构象转变。
Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy.
作者信息
Cozzone P J, Opella S J, Jardetzky O, Berthou J, Jollès P
出版信息
Proc Natl Acad Sci U S A. 1975 Jun;72(6):2095-8. doi: 10.1073/pnas.72.6.2095.
Abstract
A specific temperature-dependent conformational transition of hen egg-white lysozyme, occurring between 20 degree C and 30 degree C in solution, has been detected by 13-C-nuclear magnetic resonance spectroscopy. Selective changes in the chemical shifts of aromatic residues, together with differences in the chemical shifts, and nuclear Overhauser enhancement in the carbonyl, carboxyl, and alpha-carbon regions of the spectrum point to the vicinity of subsites D and E as the primary locus of the structural change.
摘要
通过13-C核磁共振光谱法已检测到鸡蛋清溶菌酶在溶液中20摄氏度至30摄氏度之间发生的特定温度依赖性构象转变。芳香族残基化学位移的选择性变化，以及光谱中羰基、羧基和α-碳区域化学位移的差异和核Overhauser增强，表明亚位点D和E附近是结构变化的主要位点。
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Biochemistry. 1964 Dec;3:1920-8. doi: 10.1021/bi00900a023.
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Calorimetric investigation of lysozyme thermal denaturation.
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Nuclear magnetic resonance study of the mechanism of reversible denaturation of lysozyme.溶菌酶可逆变性机制的核磁共振研究
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