Transverse relaxation-optimized HCN experiment for tautomeric states of histidine sidechains
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Function of protein is frequently related with tautomeric states of histidine sidechains. Thus, several NMR experiments were developed to determine the tautomeric states of histidines. However, poor sensitivity of these experiments caused by long duration of magnetization transfer periods is unavoidable. Here, we alleviate the sensitivity of HCN experiment for determining the tautomeric states of histidine residues using TROSY principle to suppress transverse relaxation of 13C spins during long polarization transfer delays involving 13C-15N scalar couplings. In addition, this experiment was used to assign the sidechain resonances of histidines. These assignments can be used to follow the pH-titration of histidine sidechains.
Abstract
Function of protein is frequently related with tautomeric states of histidine sidechains. Thus, several NMR experiments were developed to determine the tautomeric states of histidines. However, poor sensitivity of these experiments caused by long duration of magnetization transfer periods is unavoidable. Here, we alleviate the sensitivity of HCN experiment for determining the tautomeric states of histidine residues using TROSY principle to suppress transverse relaxation of 13C spins during long polarization transfer delays involving 13C-15N scalar couplings. In addition, this experiment was used to assign the sidechain resonances of histidines. These assignments can be used to follow the pH-titration of histidine sidechains.
참고문헌 (7)
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