Please use this identifier to cite or link to this item:
|Title:||Characterization of triple-helical conformations and melting analyses of synthetic collagen-like peptides by reversed-phase HPLC|
|Citation:||Khew, S.T., Tong, Y.W. (2007-10-15). Characterization of triple-helical conformations and melting analyses of synthetic collagen-like peptides by reversed-phase HPLC. Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences 858 (1-2) : 79-90. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jchromb.2007.08.020|
|Abstract:||There is a confusion in the application of circular dichroism (CD) spectroscopy in analyzing collagen's structure for the overlapping of the spectral shapes and positions of the collagen triple helix and poly(proline-II)-like structure. The unique repetitive sequence of the collagen triple helix is susceptible to misalignment during the spontaneous assembly. Such misaligned structures are usually difficult to be characterized by CD or NMR spectroscopy. Here, RP-HPLC was developed as a conformational characterization technique for synthetic collagen-like peptides based on the different hydrophobicities exhibited by the triple-helical and unassembled peptides. RP-HPLC was also used to study thermal transitions and to measure melting point temperatures (Tm) of the collagen-like peptides. © 2007 Elsevier B.V. All rights reserved.|
|Source Title:||Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Jul 22, 2018
WEB OF SCIENCETM
checked on Jun 19, 2018
checked on May 25, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.