Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin.

Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin.

Pressure-induced unfolding of a molten globule (MG) was studied in a residue-specific manner with (1)H-(15)N two-dimensional NMR spectroscopy using a variant of human alpha-lactalbumin (alpha-LA), in which all eight cysteines had been replaced with alanines (all-Ala alpha-LA). The NMR spectrum under...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς:	Lassalle, M, Li, H, Yamada, H, Akasaka, K, Redfield, C
Μορφή:	Journal article
Γλώσσα:	English
Έκδοση:	2003

Παρόμοια τεκμήρια

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ανά: Wijesinha-Bettoni, R, κ.ά.
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ανά: Rösner, H, κ.ά.
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ανά: Schulman, Brenda Arlene
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ανά: Last, A, κ.ά.
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ανά: Young, M, κ.ά.
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ανά: Schäfer, H, κ.ά.
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ανά: Wirmer, J, κ.ά.
Έκδοση: (2006)

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ανά: Smith, L, κ.ά.
Έκδοση: (1999)

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ανά: Smith, L, κ.ά.
Έκδοση: (1994)

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ανά: Carver, J, κ.ά.
Έκδοση: (2002)

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ανά: Redfield, C
Έκδοση: (2004)

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ανά: Olga I Povarova, κ.ά.
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ανά: Redfield, C
Έκδοση: (2004)

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ανά: Paci, E, κ.ά.
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ανά: Treweek, T, κ.ά.
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ανά: Greene, L, κ.ά.
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ανά: Higman, V, κ.ά.
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ανά: Bruylants, G, κ.ά.
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ανά: Lan Chen, κ.ά.
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ανά: Wada, Hirofumi, κ.ά.
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ανά: Wijesinha-Bettoni, R, κ.ά.
Έκδοση: (2001)

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ανά: Forge, V, κ.ά.
Έκδοση: (1999)

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ανά: Phillips, D, κ.ά.
Έκδοση: (1987)

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ανά: Scrutton, H, κ.ά.
Έκδοση: (2007)

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ανά: Di Paolo, A, κ.ά.
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ανά: Acharya, K, κ.ά.
Έκδοση: (1990)

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ανά: Ren, J, κ.ά.
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ανά: Stuart, D, κ.ά.
Έκδοση: (1986)

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