The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit.
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Involvement of C-Terminal Histidines in Soybean PM1 Protein Oligomerization and Cu2+ Binding.Group 4 late embryogenesis abundant proteins as a model to study intrinsically disordered proteins in plants.Structural disorder in plant proteins: where plasticity meets sessility.Folding of intrinsically disordered plant LEA proteins is driven by glycerol-induced crowding and the presence of membranes.Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein.
P2860
The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit.
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name
The Unstructured N-terminal Re ...... Activity under Water Deficit.
@ast
The Unstructured N-terminal Re ...... Activity under Water Deficit.
@en
type
label
The Unstructured N-terminal Re ...... Activity under Water Deficit.
@ast
The Unstructured N-terminal Re ...... Activity under Water Deficit.
@en
prefLabel
The Unstructured N-terminal Re ...... Activity under Water Deficit.
@ast
The Unstructured N-terminal Re ...... Activity under Water Deficit.
@en
P2860
P356
P1476
The Unstructured N-terminal Re ...... Activity under Water Deficit.
@en
P2093
Alejandra A Covarrubias
José Luis Reyes
P2860
P304
10893-10903
P356
10.1074/JBC.M116.720318
P407
P577
2016-03-22T00:00:00Z