Structural characterisation of the human alpha-lactalbumin molten globule at high temperature.
Molten globules are partially folded forms of proteins thought to be general intermediates in protein folding. The 15N-1H HSQC NMR spectrum of the human alpha-lactalbumin (alpha-LA) molten globule at pH 2 and 20 degrees C is characterised by broad lines which make direct study by NMR methods difficu...
Hlavní autoři: | Ramboarina, S, Redfield, C |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
2003
|
Podobné jednotky
-
Probing the effect of temperature on the backbone dynamics of the human alpha-lactalbumin molten globule.
Autor: Ramboarina, S, a další
Vydáno: (2008) -
Local and global cooperativity in the human alpha-lactalbumin molten globule.
Autor: Quezada, C, a další
Vydáno: (2004) -
Structure and determinants of the alpha-lactalbumin molten globule
Autor: Wu, Lawren Chialun, 1970-
Vydáno: (2009) -
Comparison of the denaturant-induced unfolding of the bovine and human alpha-lactalbumin molten globules.
Autor: Wijesinha-Bettoni, R, a další
Vydáno: (2001) -
Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin.
Autor: Lassalle, M, a další
Vydáno: (2003)