The effects of excipients on the structure and dynamics of insulin and the Lys(B28)Pro(B29) mutant: An NMR study.
The existence of multiple hexameric conformations of insulin has been well defined by x-ray crystallography. Insulin conformation within the hexamer has been shown to be dependent upon solution conditions, particularly, the presence of metal ions, protein concentration, pH and the presence of ligand...
Main Author: | Hardaway, Lori Ann. |
---|---|
Other Authors: | MacKenzie, Neil |
Language: | en |
Published: |
The University of Arizona.
1994
|
Online Access: | http://hdl.handle.net/10150/187246 |
Similar Items
-
Characterization of Structural, Dynamic and Functional Relationships of a Mutant Analogous from Mastoparan-B by NMR
by: Hsin-Ru Chang, et al.
Published: (2011) -
Structural characterization of the Dutch mutant of b-amyloid peptide by NMR spectroscopy
by: Chuan-Ying Tzeng, et al.
Published: (2012) -
Matriptase cleaves the amyloid-beta peptide 1–42 at Arg-5, Lys-16, and Lys-28
by: Li-Mei Chen, et al.
Published: (2019-01-01) -
Phenolic excipients of insulin formulations induce cell death, pro-inflammatory signaling and MCP-1 release
by: Claudia Weber, et al.
Published: (2015-01-01) -
Alterations in phospholipid catabolism in Mycobacterium tuberculosis lysX mutant
by: Erin A Maloney, et al.
Published: (2011-02-01)