Folding of intrinsically disordered plant LEA proteins is driven by glycerol-induced crowding and the presence of membranes.
about
Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy.Group 4 late embryogenesis abundant proteins as a model to study intrinsically disordered proteins in plants.Potential functions of LEA proteins from the brine shrimp Artemia franciscana - anhydrobiosis meets bioinformatics.Intrinsically Disordered Stress Protein COR15A Resides at the Membrane Surface during Dehydration.Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein.
P2860
Folding of intrinsically disordered plant LEA proteins is driven by glycerol-induced crowding and the presence of membranes.
description
2017 nî lūn-bûn
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name
Folding of intrinsically disor ...... and the presence of membranes.
@en
Folding of intrinsically disor ...... and the presence of membranes.
@nl
type
label
Folding of intrinsically disor ...... and the presence of membranes.
@en
Folding of intrinsically disor ...... and the presence of membranes.
@nl
prefLabel
Folding of intrinsically disor ...... and the presence of membranes.
@en
Folding of intrinsically disor ...... and the presence of membranes.
@nl
P2093
P2860
P356
P1433
P1476
Folding of intrinsically disor ...... and the presence of membranes.
@en
P2093
Anja Thalhammer
Anne Bremer
Dirk K Hincha
Martin Wolff
P2860
P304
P356
10.1111/FEBS.14023
P407
P577
2017-01-21T00:00:00Z