Serine protease inhibitor mediated peptide bond re-synthesis in diverse protein molecules
| Autor: | Amit Sharma, K. V. Radha Kishan |
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| Rok vydání: | 2011 |
| Předmět: |
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Molecular Serine Proteinase Inhibitors Protein Conformation medicine.medical_treatment Proteolysis Biophysics Biochemistry chemistry.chemical_compound Nicked protein Structural Biology Genetics medicine Animals Peptide bond Molecule Subtilisins Molecular Biology Serine protease Protease medicine.diagnostic_test biology Proteins Cell Biology PMSF Protease inhibitor (biology) Phenylmethylsulfonyl Fluoride chemistry biology.protein Religation Muramidase Peptides Subtilisin Carlsberg MASP1 medicine.drug |
| Zdroj: | FEBS Letters. 585:3465-3470 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2011.10.004 |
| Popis: | Protease inhibitors have been extensively used in research to prevent unwanted degradation of proteins during purification and analysis. Here, we report a remarkable discovery of protease inhibitor mediated reformation of peptide bonds by the serine protease inhibitor, PMSF in a diverse set of proteolyzed molecules. Interestingly, the religation reaction in the presence of PMSF occurs in a very short time period and with very high yields of the religated product. We also investigate the plausible mechanism of such a reaction and demonstrate through biochemical studies and X-ray crystallography that proximity of reacting termini is essential for the feasibility of this reaction. |
| Databáze: | OpenAIRE |
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