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本文引用的文献
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Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: neutron structure of trypsin.
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Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: hydrolyses of thiono and oxygen esters.
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Identification of the histidine residue at the active center of trypsin labelled by TLCK.
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13C NMR study of the ionizations within a trypsin-chloromethyl ketone inhibitor complex.
Biochemistry. 1985 Jul 2;24(14):3478-87. doi: 10.1021/bi00335a014.
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Do cleavages of amides by serine proteases occur through a stepwise pathway involving tetrahedral intermediates?
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Carbon-13 nuclear magnetic resonance as a probe of side chain orientation and mobility in carboxymethylated human carbonic anhydrase B.
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