Site-specific hydrogen exchange of proteins: insights into the structures of amyloidogenic intermediates.
We describe the use of nano-electrospray ionization (nano-ESI) mass spectrometry (MS) for monitoring hydrogen exchange. Using this approach, we have compared the fluctuations in structure of the wild-type human lysozyme with those of the Asp67His and Ile56Thr variants, the two amyloidogenic forms of...
Autors principals: | Yao, Z, Tito, P, Robinson, C |
---|---|
Format: | Journal article |
Idioma: | English |
Publicat: |
2005
|
Ítems similars
-
Probing conformations of amyloidogenic proteins by hydrogen exchange and mass spectrometry.
per: Nettleton, E, et al.
Publicat: (1999) -
Structural Insight of Amyloidogenic Intermediates of Human Insulin
per: Sandip Dolui, et al.
Publicat: (2018-02-01) -
The solution dynamics of amyloidogenic Asp67His variant of human lysozyme: Insights from hydrogen exchange
per: Canet, D, et al.
Publicat: (2000) -
Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: a site-specific investigation by mass spectrometry.
per: Tito, P, et al.
Publicat: (2000) -
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
per: Canet, D, et al.
Publicat: (2002)