Molecular recognition between serine proteases and new bioactive microproteins with a knotted structure

Initial Disulfide Formation Steps in the Folding of an ω-Conotoxin

“…Since each reduced analogue contains four Cys residues, these rates are consistent with previous results indicating that the rate constant for exchange between a single thiol in a positively charge peptide and GSSG under these conditions is typically about 0.5-2 s -1 M -1 (31,32). [8][9][10][11][12][13][14][15][16][17][18][19][20] 0.04 0.01 [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] 0.02 0.02 [15][16][17][18][19][20] 0.25 0.24 [15][16][17][18][19][20][21][22][23][24]…”

Initial Disulfide Formation Steps in the Folding of an ω-Conotoxin

“…Since each reduced analogue contains four Cys residues, these rates are consistent with previous results indicating that the rate constant for exchange between a single thiol in a positively charge peptide and GSSG under these conditions is typically about 0.5-2 s -1 M -1 (31,32). [8][9][10][11][12][13][14][15][16][17][18][19][20] 0.04 0.01 [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] 0.02 0.02 [15][16][17][18][19][20] 0.25 0.24 [15][16][17][18][19][20][21][22][23][24]…”

Solution structure of the main α‐amylase inhibitor from amaranth seeds

“…The disulfide bridge involving Cys17 and Cys31 passes through the closed loop made up from the Cys1±Cys8 and Cys18±Cys23 backbone segments and the Cys1±Cys18, Cys8±Cys23 disulfide bridges. This topology is consistent with that of à Cysteine-Knot' motif, generating a knottin-fold[40,42].…”

“…The spatial arrangement of the disulfide bridges into a cysteine knot ( Fig. 3), leads to the so-called knottin fold [40,42] as reported by Lu et al [8]. The well-conserved mutual orientation of the side chains of Lys4 and Trp5 explains the unusual chemical shifts of the 1 H resonances of Lys4 Table 4).…”

Solution Structure of PAFP-S: A New Knottin-Type Antifungal Peptide from the Seeds of Phytolacca americana,

“…The third bridge (Cys3-Cys20) was deduced indirectly via long-range connectivities between residues Cys20 and Ile4. The proposed disulfide pairings, Cys3-Cys20, Cys10-Cys24, and Cys19-Cys35, are fully compatible with the disulfide bond pattern found for a group of peptides collectively termed "knottins" (27). Secondary Structure.…”

Initial Disulfide Formation Steps in the Folding of an ω-Conotoxin

“…Since each reduced analogue contains four Cys residues, these rates are consistent with previous results indicating that the rate constant for exchange between a single thiol in a positively charge peptide and GSSG under these conditions is typically about 0.5-2 s -1 M -1 (31,32). [8][9][10][11][12][13][14][15][16][17][18][19][20] 0.04 0.01 [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] 0.02 0.02 [15][16][17][18][19][20] 0.25 0.24 [15][16][17][18][19][20][21][22][23][24]…”

Solution structure of the main α‐amylase inhibitor from amaranth seeds

“…The disulfide bridge involving Cys17 and Cys31 passes through the closed loop made up from the Cys1±Cys8 and Cys18±Cys23 backbone segments and the Cys1±Cys18, Cys8±Cys23 disulfide bridges. This topology is consistent with that of à Cysteine-Knot' motif, generating a knottin-fold[40,42].…”

“…The spatial arrangement of the disulfide bridges into a cysteine knot ( Fig. 3), leads to the so-called knottin fold [40,42] as reported by Lu et al [8]. The well-conserved mutual orientation of the side chains of Lys4 and Trp5 explains the unusual chemical shifts of the 1 H resonances of Lys4 Table 4).…”

Solution Structure of PAFP-S: A New Knottin-Type Antifungal Peptide from the Seeds of Phytolacca americana,

“…The third bridge (Cys3-Cys20) was deduced indirectly via long-range connectivities between residues Cys20 and Ile4. The proposed disulfide pairings, Cys3-Cys20, Cys10-Cys24, and Cys19-Cys35, are fully compatible with the disulfide bond pattern found for a group of peptides collectively termed "knottins" (27). Secondary Structure.…”

Initial Disulfide Formation Steps in the Folding of an ω-Conotoxin

“…Since each reduced analogue contains four Cys residues, these rates are consistent with previous results indicating that the rate constant for exchange between a single thiol in a positively charge peptide and GSSG under these conditions is typically about 0.5-2 s -1 M -1 (31,32). [8][9][10][11][12][13][14][15][16][17][18][19][20] 0.04 0.01 [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] 0.02 0.02 [15][16][17][18][19][20] 0.25 0.24 [15][16][17][18][19][20][21][22][23][24]…”

Solution structure of the main α‐amylase inhibitor from amaranth seeds

“…The disulfide bridge involving Cys17 and Cys31 passes through the closed loop made up from the Cys1±Cys8 and Cys18±Cys23 backbone segments and the Cys1±Cys18, Cys8±Cys23 disulfide bridges. This topology is consistent with that of à Cysteine-Knot' motif, generating a knottin-fold[40,42].…”

“…The spatial arrangement of the disulfide bridges into a cysteine knot ( Fig. 3), leads to the so-called knottin fold [40,42] as reported by Lu et al [8]. The well-conserved mutual orientation of the side chains of Lys4 and Trp5 explains the unusual chemical shifts of the 1 H resonances of Lys4 Table 4).…”

Solution Structure of PAFP-S: A New Knottin-Type Antifungal Peptide from the Seeds of Phytolacca americana,

“…The third bridge (Cys3-Cys20) was deduced indirectly via long-range connectivities between residues Cys20 and Ile4. The proposed disulfide pairings, Cys3-Cys20, Cys10-Cys24, and Cys19-Cys35, are fully compatible with the disulfide bond pattern found for a group of peptides collectively termed "knottins" (27). Secondary Structure.…”