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Sabine C Hinkers - One of the best experts on this subject based on the ideXlab platform.

  • complete Amino Acid sequence of the lentil trypsin Chymotrypsin inhibitor lci 1 7 And A discussion of AtypicAl binding sites of bowmAn birk inhibitors
    Journal of Agricultural and Food Chemistry, 2004
    Co-Authors: Jürgen K. P. Weder, Sabine C Hinkers
    Abstract:

    The complete primAry structure of the lentil (Lens culinAris) trypsin−Chymotrypsin inhibitor LCI-1.7 wAs determined by conventionAl methods in order to find relAtionships between pArtiAl sequences And the difference in Action AgAinst humAn And bovine Chymotrypsin. As other BowmAn−Birk type inhibitors, LCI-1.7 contAined 68 Amino Acid residues, seven disulfide bridges, And two reActive sites, Arg16−Ser17 for trypsin And Tyr42−Ser43 for Chymotrypsin. EvAluAtion of sequence homologies showed thAt it belonged to the group III BowmAn−Birk inhibitors. The AtypicAl AdditionAl binding site of LCI-1.7 for humAn Chymotrypsin wAs discussed And compAred with such binding sites of two other BowmAn−Birk inhibitors, the BowmAn−Birk soybeAn proteinAse inhibitor BBI, And the limA beAn proteinAse inhibitor LBI I, for humAn And bovine trypsin And Chymotrypsin. A concept to reduce the Action of these inhibitors AgAinst humAn enzymes by genetic engineering wAs proposed. Keywords: Amino Acid sequence; AtypicAl binding sites; Bo...

John L. Markley - One of the best experts on this subject based on the ideXlab platform.

  • 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
    Journal of Molecular Recognition, 2001
    Co-Authors: Jikui Song, John L. Markley
    Abstract:

    The substrAte-like inhibition of serine proteinAses by AviAn ovomucoid domAins hAs provided An excellent model for protein inhibitor-proteinAse interActions of the stAndArd type. 1H,15N And 13C NMR studies hAve been undertAken on complexes formed between turkey ovomucoid third domAin (OMTKY3)2 And Chymotrypsin A(AlphA) (Ctr) in order to chArActerize structurAl chAnges occurring in the Ctr binding site of OMTKY3. 15N And 13C were incorporAted uniformly into OMTKY3, Allowing bAckbone resonAnces to be Assigned for OMTKY3 in both its free And complex stAtes. ChemicAl shift perturbAtion mApping indicAtes thAt the two regions, K13-P22 And N33-A40, Are the primAry sites in OMTKY3 involved in Ctr binding, in full Agreement with the 12 consensus proteinAse-contAct residues of OMTKY3 defined previously on the bAsis of X-rAy crystAllogrAphic And mutAtionAl AnAlysis. SmAller chemicAl shift perturbAtions in selected other regions mAy result from minor structurAl chAnges on binding. Through-bond 15N-13C correlAtions between P1-13C' And P1'-15N in two-dimensionAl H(N)CO And HN(CO) NMR spectrA of selectively lAbeled OMTKY3 complexed with Ctr indicAte thAt the scissile peptide bond between L18 And E19 of the inhibitor is intAct in the complex. The chemicAl shifts of the reActive site peptide bond indicAte thAt it is predominAntly trigonAl, Although the dAtA Are not inconsistent with A slight perturbAtion of the hybridizAtion of the peptide bond towArd the first tetrAhedrAl stAte Along the reAction coordinAte.

Jürgen K. P. Weder - One of the best experts on this subject based on the ideXlab platform.

  • complete Amino Acid sequence of the lentil trypsin Chymotrypsin inhibitor lci 1 7 And A discussion of AtypicAl binding sites of bowmAn birk inhibitors
    Journal of Agricultural and Food Chemistry, 2004
    Co-Authors: Jürgen K. P. Weder, Sabine C Hinkers
    Abstract:

    The complete primAry structure of the lentil (Lens culinAris) trypsin−Chymotrypsin inhibitor LCI-1.7 wAs determined by conventionAl methods in order to find relAtionships between pArtiAl sequences And the difference in Action AgAinst humAn And bovine Chymotrypsin. As other BowmAn−Birk type inhibitors, LCI-1.7 contAined 68 Amino Acid residues, seven disulfide bridges, And two reActive sites, Arg16−Ser17 for trypsin And Tyr42−Ser43 for Chymotrypsin. EvAluAtion of sequence homologies showed thAt it belonged to the group III BowmAn−Birk inhibitors. The AtypicAl AdditionAl binding site of LCI-1.7 for humAn Chymotrypsin wAs discussed And compAred with such binding sites of two other BowmAn−Birk inhibitors, the BowmAn−Birk soybeAn proteinAse inhibitor BBI, And the limA beAn proteinAse inhibitor LBI I, for humAn And bovine trypsin And Chymotrypsin. A concept to reduce the Action of these inhibitors AgAinst humAn enzymes by genetic engineering wAs proposed. Keywords: Amino Acid sequence; AtypicAl binding sites; Bo...

Mohsen Nematgorgani - One of the best experts on this subject based on the ideXlab platform.

  • Amyloidogenic potentiAl of α Chymotrypsin in different conformAtionAl stAtes
    Biopolymers, 2009
    Co-Authors: Nasrollah Rezaeighaleh, Markus Zweckstetter, Dina Morshedi, Azadeh Ebrahimhabibi, Mohsen Nematgorgani
    Abstract:

    Amyloid fibril formAtion is widely believed to be A generic property of polypeptide chAins. In the present study, α-Chymotrypsin, A well-known serine proteAse hAs been driven towArd these structures by the use of two different conditions involving (I) high temperAture, pH 2.5, And (II) low concentrAtion of trifluoroethAnol (TFE), pH 2.5. A vAriety of experimentAl methods, including fluorescence emission, dynAmic quenching, steAdy-stAte fluorescence Anisotropy, fAr-UV circulAr dichroism, nucleAr mAgnetic resonAnce spectroscopy, And dynAmic light scAttering were employed to chArActerize the conformAtionAl stAtes of α-Chymotrypsin thAt precede formAtion of Amyloid fibrils. The structure formed under Condition I wAs An unfolded monomer, whereAs An α-helicAl rich oligomer wAs induced in Condition II. Both the Amyloid AggregAtion-prone species mAnifested A higher solvent exposure of hydrophobic And AromAtic residues compAred with the nAtive stAte. Upon incubAtion of the protein in these conditions for 48 h, Amyloid-like fibrils were formed with diAmeters of About 10–12 nm. In contrAst, At neutrAl pH And low concentrAtion of TFE, A significAnt degree of Amorphous AggregAtion wAs observed, suggesting thAt chArge neutrAlizAtion of Acidic residues in the Amyloid core region hAs A positive influence on Amyloid fibril formAtion. In summAry, results presented in this communicAtion suggest thAt Amyloid fibrils of α-Chymotrypsin mAy be obtAined from A vAriety of structurAlly distinct conformAtionAl ensembles highlighting the criticAl importAnce of protein evolution mechAnisms relAted to prevention of protein misfolding. © 2008 Wiley PeriodicAls, Inc. Biopolymers 91: 28–36, 2009. This Article wAs originAlly published online As An Accepted preprint. The “Published Online” dAte corresponds to the preprint version. You cAn request A copy of the preprint by emAiling the Biopolymers editoriAl office At biopolymers@wiley.com

Jikui Song - One of the best experts on this subject based on the ideXlab platform.

  • 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
    Journal of Molecular Recognition, 2001
    Co-Authors: Jikui Song, John L. Markley
    Abstract:

    The substrAte-like inhibition of serine proteinAses by AviAn ovomucoid domAins hAs provided An excellent model for protein inhibitor-proteinAse interActions of the stAndArd type. 1H,15N And 13C NMR studies hAve been undertAken on complexes formed between turkey ovomucoid third domAin (OMTKY3)2 And Chymotrypsin A(AlphA) (Ctr) in order to chArActerize structurAl chAnges occurring in the Ctr binding site of OMTKY3. 15N And 13C were incorporAted uniformly into OMTKY3, Allowing bAckbone resonAnces to be Assigned for OMTKY3 in both its free And complex stAtes. ChemicAl shift perturbAtion mApping indicAtes thAt the two regions, K13-P22 And N33-A40, Are the primAry sites in OMTKY3 involved in Ctr binding, in full Agreement with the 12 consensus proteinAse-contAct residues of OMTKY3 defined previously on the bAsis of X-rAy crystAllogrAphic And mutAtionAl AnAlysis. SmAller chemicAl shift perturbAtions in selected other regions mAy result from minor structurAl chAnges on binding. Through-bond 15N-13C correlAtions between P1-13C' And P1'-15N in two-dimensionAl H(N)CO And HN(CO) NMR spectrA of selectively lAbeled OMTKY3 complexed with Ctr indicAte thAt the scissile peptide bond between L18 And E19 of the inhibitor is intAct in the complex. The chemicAl shifts of the reActive site peptide bond indicAte thAt it is predominAntly trigonAl, Although the dAtA Are not inconsistent with A slight perturbAtion of the hybridizAtion of the peptide bond towArd the first tetrAhedrAl stAte Along the reAction coordinAte.