Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Terrance J. Sereda"'
Publikováno v:
Acta Biomaterialia.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cf7fa8d3fe29de5c6ba692fdf13e17df
https://doi.org/10.1016/j.actbio.2023.05.009
https://doi.org/10.1016/j.actbio.2023.05.009
Publikováno v:
Journal of Chromatography A. 776:153-165
The reversed-phase liquid chromatography (RPLC) behavior of synthetic model peptides containing positively charged amino acid residues was studied in the presence or absence of 100 mM sodium perchlorate in order to determine the effect on apparent si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::af1ef689a5f02021c113fc8cdce34b6f
https://doi.org/10.1016/s0021-9673(97)00150-7
https://doi.org/10.1016/s0021-9673(97)00150-7
Publikováno v:
Journal of Peptide Science. 1:319-329
The aim of the present investigation is to determine the effect of alpha-helical propensity and sidechain hydrophobicity on the stability of amphipathic alpha-helices. Accordingly, a series of 18-residue amphipathic alpha-helical peptides has been sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19d0fec382d3c1709c4e6e4b5dcaa451
https://doi.org/10.1002/psc.310010507
https://doi.org/10.1002/psc.310010507
Publikováno v:
Journal of Chromatography A. 695:205-221
The reversed-phase retention behaviour of two series of peptides, one non-helical and the other alpha-helical, was studied under various linear AB gradients in order to determine the effect of peptide conformation on selectivity of the separation. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3af0e374a3792e32ae8e0dd147bcd379
https://doi.org/10.1016/0021-9673(94)01147-7
https://doi.org/10.1016/0021-9673(94)01147-7
Publikováno v:
Journal of Chromatography A. 676:139-153
To mimic a hydrophobic protein binding domain, which is a region on the surface of a protein that has a preference or a specificity to interact with a complementary surface, we have designed amphipathic α-helical peptides where the non-polar face in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a19dbcc6a152b5f07bb6465fa0378a0
https://doi.org/10.1016/0021-9673(94)00371-8
https://doi.org/10.1016/0021-9673(94)00371-8
Publikováno v:
Journal of chromatography. 646(1)
We have examined the contribution of the alpha-amino group to retention behaviour for peptides in reversed-phase chromatography using two series of peptide analogues, one containing an N alpha-acetylated terminal and the other containing an alpha-ami
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35ae3ba48af4bd88bd382e6a9191e497
https://pubmed.ncbi.nlm.nih.gov/8408425
https://pubmed.ncbi.nlm.nih.gov/8408425