Determining the native and nonnative effects of myristoylation on the folding and switching of hisactophilin
Myristoylation, the covalent linkage of a C14 saturated fatty acyl chain to the N-terminal glycine in a protein, plays an important role in reversible membrane and protein binding in cellular signaling by the modified proteins. Little is known about the effects of myristoylation on the energetics a...
Main Author: | Smith, Martin Thomas James |
---|---|
Language: | en |
Published: |
2012
|
Subjects: | |
Online Access: | http://hdl.handle.net/10012/7016 |
Similar Items
-
Determining the native and nonnative effects of myristoylation on the folding and switching of hisactophilin
by: Smith, Martin Thomas James
Published: (2012) -
Effects of Myristoylation on the Structure and Stability of Hisactophilin
by: Meissner, Joseph
Published: (2007) -
Effects of Myristoylation on the Structure and Stability of Hisactophilin
by: Meissner, Joseph
Published: (2007) -
Role of Symmetry in Hisactophilin Folding
by: Ghashut, Fadila
Published: (2009) -
Role of Symmetry in Hisactophilin Folding
by: Ghashut, Fadila
Published: (2009)