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2000 | 1 |
2001 | 2 |
2024 | 0 |
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Formation of a noncovalent serpin-proteinase complex involves no conformational change in the serpin. Use of 1H-15N HSQC NMR as a sensitive nonperturbing monitor of conformation.
Biochemistry. 2000 Oct 3;39(39):11884-92. doi: 10.1021/bi001152+.
Biochemistry. 2000.
PMID: 11009600
High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy.
Peterson FC, Gordon NC, Gettins PG.
Peterson FC, et al.
Biochemistry. 2001 May 29;40(21):6275-83. doi: 10.1021/bi0100992.
Biochemistry. 2001.
PMID: 11371189
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Insight into the mechanism of serpin-proteinase inhibition from 2D [1H-15N] NMR studies of the 69 kDa alpha 1-proteinase inhibitor Pittsburgh-trypsin covalent complex.
Peterson FC, Gettins PG.
Peterson FC, et al.
Biochemistry. 2001 May 29;40(21):6284-92. doi: 10.1021/bi010100x.
Biochemistry. 2001.
PMID: 11371190
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