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1.
Modeling of the Peptide Release during Proteolysis of ß-Lactoglobulin by Trypsin with Consideration of Peptide Bond Demasking.
Int J Mol Sci
; 24(15)2023 Jul 25.
Artículo
en Inglés
| MEDLINE | ID: mdl-37569305
2.
Proteolysis of Micellar ß-Casein by Trypsin: Secondary Structure Characterization and Kinetic Modeling at Different Enzyme Concentrations.
Int J Mol Sci
; 24(4)2023 Feb 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-36835285
3.
Modeling of Proteolysis of ß-Lactoglobulin and ß-Casein by Trypsin with Consideration of Secondary Masking of Intermediate Polypeptides.
Int J Mol Sci
; 23(15)2022 Jul 22.
Artículo
en Inglés
| MEDLINE | ID: mdl-35897664
4.
A straightforward kinetic evidence for coexistence of "induced fit" and "selected fit" in the reaction mechanism of a mutant tryptophan indole lyase Y72F from Proteus vulgaris.
Biochim Biophys Acta
; 1844(10): 1860-7, 2014 Oct.
Artículo
en Inglés
| MEDLINE | ID: mdl-25084024
5.
Methionine gamma-lyase: mechanistic deductions from the kinetic pH-effects. The role of the ionic state of a substrate in the enzymatic activity.
Biochim Biophys Acta
; 1794(10): 1414-20, 2009 Oct.
Artículo
en Inglés
| MEDLINE | ID: mdl-19501676
6.
Proteolytically-induced changes of secondary structural protein conformation of bovine serum albumin monitored by Fourier transform infrared (FT-IR) and UV-circular dichroism spectroscopy.
Spectrochim Acta A Mol Biomol Spectrosc
; 161: 8-18, 2016 May 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-26926394
7.
Real time observation of proteolysis with Fourier transform infrared (FT-IR) and UV-circular dichroism spectroscopy: watching a protease eat a protein.
Spectrochim Acta A Mol Biomol Spectrosc
; 79(1): 104-11, 2011 Jun.
Artículo
en Inglés
| MEDLINE | ID: mdl-21398173
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