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The Mycobacterium leprae hsp65 displays proteolytic activity. Mutagenesis studies indicate that the M. leprae hsp65 Proteolytic activity is catalytically related to the HslVU protease?
(2002-06-11)
The present study reports, for the first time, that the recombinant hsp65 from Mycobacterium leprae (chaperonin 2) displays a proteolytic activity toward oligopeptides. The M. leprae hsp65 proteolytic activity revealed a ...
The stereochemistry of the addition of titanium enolates of N-propionyl-oxazolidin-2-ones to 5- and 6-membered N-acyliminium ions
(Pergamon-elsevier Science LtdOxfordInglaterra, 1999)
A SequenceSpace analysis of Lys49 phospholipases A2: Clues towards identification of residues involved in a novel mechanism of membrane damage and in myotoxicity
(1998-04-01)
'SequenceSpace' analysis is a novel approach which has been used to identify unique amino acids within a subfamily of phospholipases A2 (PLA2) in which the highly conserved active site residue Asp49 is substituted by Lys ...
A SequenceSpace analysis of Lys49 phospholipases A2: Clues towards identification of residues involved in a novel mechanism of membrane damage and in myotoxicity
(1998-04-01)
'SequenceSpace' analysis is a novel approach which has been used to identify unique amino acids within a subfamily of phospholipases A2 (PLA2) in which the highly conserved active site residue Asp49 is substituted by Lys ...
Chiral transmission between amino acids: Chirally selective amino acid substitution in the serine octamer as a possible step in homochirogenesis
(Wiley-v C H Verlag GmbhWeinheimAlemanha, 2002)
Erratum: Publisher Correction: Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements
(2018)
Why is an amino acid replacement in a protein accepted during evolution? The answer given by bioinformatics relies on the frequency of change of each amino acid by another one and the propensity of each to remain unchanged. ...
Mass and secondary structure propensity of amino acids explain their mutability and evolutionary replacements
Why is an amino acid replacement in a protein accepted during evolution? The answer given by bioinformatics relies on the frequency of change of each amino acid by another one and the propensity of each to remain unchanged. ...
Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements (vol 7, 7717, 2017)
Why is an amino acid replacement in a protein accepted during evolution? The answer given by bioinformatics relies on the frequency of change of each amino acid by another one and the propensity of each to remain unchanged. ...