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Wednesday, August 5, 2020 | History

2 edition of 13C-NMR study of tetrahedral adducts with chymotrypsin and subtilisin BPN found in the catalog.

13C-NMR study of tetrahedral adducts with chymotrypsin and subtilisin BPN

Timothy P. O"Connell

13C-NMR study of tetrahedral adducts with chymotrypsin and subtilisin BPN

by Timothy P. O"Connell

  • 163 Want to read
  • 20 Currently reading

Published by University College Dublin in Dublin .
Written in English

    Subjects:
  • Nuclear magnetic resonance.,
  • Chymotrypsin.

  • Edition Notes

    Statementby Timothy P. O"Connell.
    ContributionsUniversity College Dublin. Department of Biochemistry.
    The Physical Object
    Paginationxii, 276p. :
    Number of Pages276
    ID Numbers
    Open LibraryOL17484782M

      1. Arch Biochem Biophys. Jan 15;(1) A kinetic investigation of subsites S1' and S2' in alpha-chymotrypsin and subtilisin BPN'.Cited by: J. Mol. Biol. () , Role of Catalytic Residues in the Formation of a Tetrahedral Adduct in the Acylation Reaction of Bovine Trypsin A Molecular Orbital Study SETSUKO NAKAGAWA AND HTDEAKI EYAMA+ School of Pharmaceutical Sciences, Kitasato University Shirokane, Minato-ku, Toyko , Japan (Received 17 October , and in revised form 25 May ) In the acylation reaction of Cited by:

    Subtilisin. Stereochemical mechanism involving transition-state stabilizationCited by:   Finucane MD, Malthouse JP. A study of the stabilization of tetrahedral adducts by trypsin and delta-chymotrypsin. Biochem J. Sep 15; (Pt 3)– [PMC free article] O'Connell TP, Malthouse JP. A study of the stabilization of the oxyanion of tetrahedral adducts by trypsin, chymotrypsin and subtilisin.

    The work uses MD simulation to study effects of five water contents (3 %, 10 %, 20 %, 50 %, % v/v) on the tetrahedral intermediate of chymotrypsin - trifluoromethyl ketone in polar acetonitrile and non-polar hexane media. The water content induced changes in the structure of the intermediate, solvent distribution and H-bonding are analyzed in the two organic by: 6. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized by:


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13C-NMR study of tetrahedral adducts with chymotrypsin and subtilisin BPN by Timothy P. O"Connell Download PDF EPUB FB2

Using 13 C NMR, we have shown that all except one of these inhibitors forms a tetrahedral adduct with chymotrypsin, subtilisin, and trypsin. From the pH-dependent changes in the chemical shift of the hemiketal carbon of the tetrahedral adduct, we are able to determine the oxyanion p K a in the different inhibitor by: 9.

A 13C-NMR study of the role of Asn in stabilizing the oxyanion of a subtilisin tetrahedral adduct. T P O'connell, R M Day, E V Torchilin, W W Bachovchin, and J G Malthouse Department of Biochemistry, University College Dublin, Dublin 4, by: 13C NMR Study of How the Oxyanion pKa Values of Subtilisin and Chymotrypsin Tetrahedral Adducts Are Affected by Different Amino Acid Residues Binding in Enzyme Subsites S1−S4.

Biochemistry38 (19), Cited by:   Abstract. delta-Chymotrypsin has been alkylated by C- and C-enriched tosylphenylalanylchloromethane. In the intact inhibitor derivative, signals due to the C- and C-enriched carbon atoms have chemical shifts which titrate from to p.p.m.

and from to p.p.m. respectively with similar pKa values of and by: 13C NMR Study of How the Oxyanion pKa Values of Subtilisin and Chymotrypsin Tetrahedral Adducts Are Affected by Different Amino Acid Residues Binding in Enzyme Subsites S1−S4. Biochemistry38 (19), DOI: /bic. Robert L. Kogan and Thomas H.

by: 13C NMR Study of How the Oxyanion pKa Values of Subtilisin and Chymotrypsin Tetrahedral Adducts Are Affected by Different Amino Acid Residues Binding in Enzyme Subsites S1−S4.

Biochemistry38 (19), DOI: /bic. Glocker, M. Kalkum, R. Yamamoto, and, J. by: Biochem. ()(Printed in Great Britain) Astudy of the stabilization of the oxyanion of tetrahedral adducts by trypsin, chymotrypsin and subtilisin Timothy P.

O'CONNELL and J. Subtilisin BPN′ (crystallized and J.J. Milne, T.P. Fitzpatrick, J.P.G. MalthouseA 13C-NMR study of how the oxyanion pK a values of subtilisin and chymotrypsin tetrahedral adducts are affected by different amino acid residues binding in enzymes subsites S1–S4.

Cited by: BTFPBA and its tetrahedral a-chymotrypsin and subtilisin adducts is probably a slow exchange process at room temperature (k tetrahedral complexes can be observed by llB NMR. Moreover, the linewidths of the bound species were.

X-Ray crystallographic study of boronic acid adducts with subtilisin BPN’ (Novo). A chemical and crystallographic study of carbamyl-chymotrypsin A. Biochemis CrossRef S. K.; Scott, A. I.; and Malthouse, P. 13C NMR study of the stereospecificity of the thiohemiacetals formed on inhibition of papain by specific.

A 13C-NMR study of the inhibition of delta-chymotrypsin by a tripeptide-glyoxal inhibitor, (). A 13C-NMR study of the role of Asn in stabilizing the oxyanion of a subtilisin tetrahedral adduct.

A study of the stabilization of tetrahedral adducts by trypsin and δ-chymotrypsin κ and α forms of chymotrypsin. 13C NMR has shown [O'Connell & Malthouse (). Biochem. subtilisin BPN.

Subtilisin BPN' has been alkylated using benzyloxycarbonyl-glycylglycyl[C]phenylalanylchloromethane+ ++. Using difference 13C-NMR spectroscopy a single signal due to the 13C-enriched alpha. Subtilisin and delta-chymotrypsin have been alkylated using C-enriched benzyloxycarbonylglycylglycylphenylalanylchloromethane.

A single signal due to the 13C-enriched carbon was detected in. 13 C NMR Study of How the Oxyanion p K a Values of Subtilisin and Chymotrypsin Tetrahedral Adducts Are Affected by Different Amino Acid Residues Binding in Enzyme Subsites S 1 −S 4 †.

Subtilisin and delta-chymotrypsin have been alkylated using C-enriched benzyloxycarbonylglycylglycylphenylalanylchloromethane. A single signal due to the 13C-enriched carbon was detected in both the intact subtilisin and delta-chymotrypsin by: J.

Paul G. Malthouse & Jennifer Alison Cleary () Using 13C-NMR to study tetrahedral inhibitor adducts formed with chymotrypsin. [Poster Presentation], 28 International Conference on Magnetic Resonance in Biological Systems, Kyoto International Conference Center, Japan, AUG.

THE JOURNAL OF &OLOGICAL CHEMISTRY 0 by The American Soeiety of Biological Chemists, Inc. Vol.No. 16, Issue of June 5, pp.Printed in U.S.A. Structure of a Tetrahedral Transition State Complex of a-Chymotrypsin Dimer at A Resolution* (Received for publication, Septem ) Alexander Tulinsky From the Department of Chemistry, Michigan State.

Step 2: Chymotrypsin Mechanism - Tetrahedral Intermediate with His57 ionized. A postulated stationary point in the reaction of Ser with the peptide bond to form the Zwitterionic tetrahedral intermediate involves the migration of the hydroxyl proton to.

Mol. Biol. () 67, Comparison of the Active Site Stereochemistry and Substrate Conformation in a-Chymotrypsin and SubtiUsin BPN' CHBISTrNE SCHTTBEET WEIGHTf Medical Research Council Laboratory of Molecular Biology Hills Boad, Cambridge CB2 2QH, England {Received 24 Augustand in revised form 20 November ) The main-chain conformation in the immiate Cited by:.

Step 3: Chymotrypsin Mechanism - the Tetrahedral Intermediate This structure can be summarized as follows: Ser has reacted with the substrate, forming a covalent bond with the carbonyl carbon of Trp, and the hydroxyl hydrogen atom that had been on Ser has now migrated to the nitrogen atom of the CH 3 -NH- group at the Trp end of the.Physical Properties.

Molecular Weight: 25 kDa 1 (Bovine) pI: (Bovine) Extinction coefficient: E1%= (nm) Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen. α-Chymotrypsin is the predominant form of active enzyme produced from it's zymogen, Chymotrypsinogen A.Welcome to Research Repository UCD Research Repository UCD is a digital collection of open access scholarly research publications from University College Dublin.

Research Repository UCD collects, preserves and makes freely available publications including peer-reviewed articles, working papers and conference papers created by UCD researchers.