Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride.
We have studied the conformational stability of the two homologous membrane skeletal proteins, the erythroid and non-erythroid spectrins, in their dimeric and tetrameric forms respectively during unfolding in the presence of urea and guanidine hydrochloride (GuHCl). Fluorescence and circular dichroi...
Main Authors: | Malay Patra, Chaitali Mukhopadhyay, Abhijit Chakrabarti |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2015-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC4305312?pdf=render |
Similar Items
-
The Role of Nonerythroid Spectrin αII in Cancer
by: Anne Ackermann, et al.
Published: (2019-01-01) -
Spectroscopic Studies on Unfolding Processes of Apo-Neuroglobin Induced by Guanidine Hydrochloride and Urea
by: Cui Zhang, et al.
Published: (2013-01-01) -
Denaturation study of N-carbamoyl-D-amino acid amidohydrolase with urea and guanidine hydrochloride
by: Chia-yu Chou, et al.
Published: (2008) -
Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates.
by: Olga I Povarova, et al.
Published: (2010-11-01) -
Aqueous solution of poly (hexamethylene guanidine hydrochloride) and poly (diethylenamine guanidine hydrochloride) as studied with acid-base indicators
by: Anastasia Yu. Kharchenko, et al.
Published: (2019-12-01)