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当S自旋磁化矢量偏离平衡态时,自旋磁化矢量将会改变,I旋磁化矢量改变速率的大小与 交互驰豫速率O1s以及S自旋磁化矢量偏离平衡态的大小成正比,I自旋磁化矢量的改变表现在S自旋受干扰时I自旋强度的改变
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1.在外磁场中核磁矩的运动规律 2.旋转坐标系 3.弛豫 4. Bloch方程
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一、在大规模测序完成后蛋白质科学成为新的科学前沿。 二、蛋白质是生物学功能的主要承担者
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一、基本要求 二、毛细管气相色谱分析法 三、手性药物的液相色谱分析法 四、核磁共振光谱分析法 五、气相色谱-质谱联用技术
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Dictionary A chemical-shift reference is used to define the (CH3)4SI positions of the resonances in the spectrum in terms of parts-per-million, or ppm, of frequency It is a material which is often directly added to the
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3. 1 Chemical shift When an atom is placed in a magnetic field B its electrons circulate about the direction of the applied magnetic field. This circulation causes a small magnetic field at the nucleus which opposes the externally applied field The magnetic field at the nucleus(the effective field) is therefore generally less than the applied field by a fraction THNMR
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A remarkab|efie|d e One of the two leading technologies in structural biolog y Great contributions to biology A special window to the development of modern structural biology and biophysics THNMR YAN
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NMR supplement The second decade into the third millenium Kurt Wuthrich NMR spectroscopy is one of the principal experimental techniques of structural biology, with abilities to determine atomic resolution structures as well as investigate dynamics and intermolecular interactions of
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MACINETIC RESONANCE ELSEVIER Progress in Nuclear Magnetic Resonance Spectroscopy 32(1998)287-387 The use of nmr methods for conformational studies of nucleic acids Sybren S. Wijmenga*, Bernd N M. van Buuren Umed University, Department of Medical Biochemistry and Biophysics, S 90187 Umed, Sweden
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NMR spectroscopy in structure-based drug design Gordon CK Roberts NMR methods for the study of motion in proteins continue Structure and dynamics of the binding site improve, and a n d complexes Methodological developments in NMR of macromolecules relevant to drug design
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