57271-88-2Relevant articles and documents
Influence of Sulfoxide Group Placement on Polypeptide Conformational Stability
Gharakhanian, Eric G.,Bahrun, Ehab,Deming, Timothy J.
supporting information, p. 14530 - 14533 (2019/10/02)
The synthesis of a homologous series containing five new nonionic sulfoxide containing polypeptides was described. Sulfoxide groups bestowed water solubility for all homologues, which allowed their use as a model for study of helix-coil transitions in water while avoiding contributions from charged groups or phase separation. Polypeptides were found to adopt chain conformations in water that were dependent on distance of sulfoxides from chain backbones, overall side-chain lengths, and solvent. These results allow preparation of polypeptide segments with different chain conformations without changing chemical functionality for potential use in structural studies and functional applications.
L-Methionine related 1-amino acids by acylase cleavage of their corresponding N-acetyl-DL-derivatives
Bommarius, Andreas S.,Drauz, Karlheinz,Guenther, Kurt,Knaup, Guenter,Schwarm, Michael
, p. 3197 - 3200 (2007/10/03)
Acylase I from Aspergillus oryzae is an even more useful enzyme than suggested so far. Besides standard amino acids such as L-Met, L-Val and L-Phe, a number of additional sulfur- and selenium-containing amino acids can be obtained at useful reaction rates and in very high enantiomeric purity by kinetic resolution of the respective N-acetyl-DL-amino acids.