fr-901724 and Gram-Positive-Bacterial-Infections

fr-901724 has been researched along with Gram-Positive-Bacterial-Infections* in 1 studies

Other Studies

1 other study(ies) available for fr-901724 and Gram-Positive-Bacterial-Infections

Article	Year
Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism. Physical chemistry chemical physics : PCCP, 2013, Jan-14, Volume: 15, Issue:2 The suitability of synchrotron radiation circular dichroism spectroscopy (SRCD) for studying interactions between the tricyclic peptide inhibitor siamycin I and the intact FsrC membrane sensor kinase in detergent micelles has been established. In the present study, tertiary structural changes demonstrate that inhibitor binding occurs at a different, non-overlapping site to the native ligand, GBAP. Topics: Amino Acid Sequence; Bacterial Proteins; Circular Dichroism; Enterococcus faecalis; Gram-Positive Bacterial Infections; Intercellular Signaling Peptides and Proteins; Molecular Sequence Data; Peptides; Protein Structure, Tertiary	2013

Article

Year

Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism.

Physical chemistry chemical physics : PCCP, 2013, Jan-14, Volume: 15, Issue:2

The suitability of synchrotron radiation circular dichroism spectroscopy (SRCD) for studying interactions between the tricyclic peptide inhibitor siamycin I and the intact FsrC membrane sensor kinase in detergent micelles has been established. In the present study, tertiary structural changes demonstrate that inhibitor binding occurs at a different, non-overlapping site to the native ligand, GBAP.

Topics: Amino Acid Sequence; Bacterial Proteins; Circular Dichroism; Enterococcus faecalis; Gram-Positive Bacterial Infections; Intercellular Signaling Peptides and Proteins; Molecular Sequence Data; Peptides; Protein Structure, Tertiary

2013