C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN

RICHARZ R, Tschesche H, WUTHRICH K (1980)
BIOCHEMISTRY 19(25): 5711-5715.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
RICHARZ, R; Tschesche, HaraldUniBi; WUTHRICH, K
Einrichtung
Fakultät für Chemie > Biochemie I
Erscheinungsjahr
1980
Zeitschriftentitel
BIOCHEMISTRY
Band
19
Ausgabe
25
Seite(n)
5711-5715
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1662058

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RICHARZ R, Tschesche H, WUTHRICH K. C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN. BIOCHEMISTRY. 1980;19(25):5711-5715.
RICHARZ, R., Tschesche, H., & WUTHRICH, K. (1980). C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN. BIOCHEMISTRY, 19(25), 5711-5715. https://doi.org/10.1021/bi00566a007
RICHARZ, R, Tschesche, Harald, and WUTHRICH, K. 1980. “C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN”. BIOCHEMISTRY 19 (25): 5711-5715.
RICHARZ, R., Tschesche, H., and WUTHRICH, K. (1980). C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN. BIOCHEMISTRY 19, 5711-5715.
RICHARZ, R., Tschesche, H., & WUTHRICH, K., 1980. C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN. BIOCHEMISTRY, 19(25), p 5711-5715.
R. RICHARZ, H. Tschesche, and K. WUTHRICH, “C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN”, BIOCHEMISTRY, vol. 19, 1980, pp. 5711-5715.
RICHARZ, R., Tschesche, H., WUTHRICH, K.: C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN. BIOCHEMISTRY. 19, 5711-5715 (1980).
RICHARZ, R, Tschesche, Harald, and WUTHRICH, K. “C-13 NUCLEAR MAGNETIC-RESONANCE STUDIES OF THE SELECTIVELY ISOTOPE-LABELED REACTIVE SITE PEPTIDE-BOND OF THE BASIC PANCREATIC TRYPSIN-INHIBITOR IN THE COMPLEXES WITH TRYPSIN, TRYPSINOGEN, AND ANHYDROTRYPSIN”. BIOCHEMISTRY 19.25 (1980): 5711-5715.

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PMID: 28495511
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Wang Y, Monzingo AF, Hu S, Schaller TH, Robertus JD, Fast W., Biochemistry 48(36), 2009
PMID: 19663506
Functional and structural roles of the Cys14-Cys38 disulfide of bovine pancreatic trypsin inhibitor.
Zakharova E, Horvath MP, Goldenberg DP., J Mol Biol 382(4), 2008
PMID: 18692070
Rigidification of a flexible protease inhibitor variant upon binding to trypsin.
Hanson WM, Domek GJ, Horvath MP, Goldenberg DP., J Mol Biol 366(1), 2007
PMID: 17157870
NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
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PMID: 11391787
Properties of the His57-Asp102 dyad of rat trypsin D189S in the zymogen, activated enzyme, and alpha1-proteinase inhibitor complexed forms.
Kaslik G, Westler WM, Gráf L, Markley JL., Arch Biochem Biophys 362(2), 1999
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Deuterium labelling in NMR structural analysis of larger proteins.
LeMaster DM., Q Rev Biophys 23(2), 1990
PMID: 2188279
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McPhalen CA, Svendsen I, Jonassen I, James MN., Proc Natl Acad Sci U S A 82(21), 1985
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Cryoenzymology of trypsin. 13C-n.m.r. detection of an acyl-trypsin intermediate in the trypsin-catalysed hydrolysis of a highly specific substrate at subzero temperature.
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PMID: 6350001
Current problems in mechanistic studies of serine and cysteine proteinases.
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PMID: 6758764
Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation.
Bolognesi M, Gatti G, Menagatti E, Guarneri M, Marquart M, Papamokos E, Huber R., J Mol Biol 162(4), 1982
PMID: 7169635
Lack of evidence for a tetrahedral intermediate in the hydrolysis of nitroanilide substrates by serine proteinases. Subzero-temperature stopped-flow experiments.
Markley JL, Travers F, Balny C., Eur J Biochem 120(3), 1981
PMID: 6460615
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