Nelson D J, Opella S J, Jardetzky O
Biochemistry. 1976 Dec 14;15(25):5552-60. doi: 10.1021/bi00670a020.
13C nuclear magnetic resonance is used to detect the Ca2+ ion controlled conformational transition in muscle calcium binding parvalbumin and to study its intramolecular motions. Nuclear relaxation parameters are used to evaluate the reorientation rates of the protein and some of the amino acid side chains. While peripheral residues exhibit greater motional freedom than the protein interior, an interesting finding is that significant rapid internal motion is present in the phenylalanine rings comprising the hydrophobic core of the protein.
13C核磁共振用于检测肌肉钙结合小清蛋白中Ca2+离子控制的构象转变，并研究其分子内运动。核弛豫参数用于评估蛋白质和一些氨基酸侧链的重排速率。虽然外周残基比蛋白质内部表现出更大的运动自由度，但一个有趣的发现是，在构成蛋白质疏水核心的苯丙氨酸环中存在显著的快速内部运动。
