scholarly journals Membrane-induced folding of the plant-stress protein Lti30.

2016 ◽  
pp. pp.01531.2015 ◽  
Author(s):  
Sylvia Eriksson ◽  
Nadejda Eremina ◽  
Andreas Barth ◽  
Jens Danielsson ◽  
Pia Harryson
Keyword(s):  
Plant Stress ◽  
Stress Protein ◽  
Induced Folding

scholarly journals The Sequence, Structure and Function of the Plant Stress Protein LEA3

2021 ◽  
Vol 120 (3) ◽  
pp. 32a
Author(s):  
Karamjeet K. Singh ◽  
Steffen P. Graether
Keyword(s):  
Plant Stress ◽  
Stress Protein ◽  
Structure And Function ◽  
Sequence Structure ◽  
And Function

scholarly journals Tunable Membrane Binding of the Intrinsically Disordered Dehydrin Lti30, a Cold-Induced Plant Stress Protein

2011 ◽  
Vol 23 (6) ◽  
pp. 2391-2404 ◽  
Author(s):  
Sylvia K. Eriksson ◽  
Michael Kutzer ◽  
Jan Procek ◽  
Gerhard Gröbner ◽  
Pia Harryson
Keyword(s):  
Plant Stress ◽  
Membrane Binding ◽  
Stress Protein ◽  
Intrinsically Disordered

scholarly journals Effect of an Intrinsically Disordered Plant Stress Protein on the Properties of Water

2018 ◽  
Vol 115 (9) ◽  
pp. 1696-1706 ◽  
Author(s):  
Luisa A. Ferreira ◽  
Alicyia Walczyk Mooradally ◽  
Boris Zaslavsky ◽  
Vladimir N. Uversky ◽  
Steffen P. Graether
Keyword(s):  
Plant Stress ◽  
Stress Protein ◽  
Intrinsically Disordered

PSPDB: Plant Stress Protein Database

2014 ◽  
Vol 32 (4) ◽  
pp. 940-942 ◽  
Author(s):  
S. Anil Kumar ◽  
P. Hima Kumari ◽  
Vijayaraghava Seshadri Sundararajan ◽  
Prashanth Suravajhala ◽  
Rajaraman Kanagasabai ◽  
...  
Keyword(s):  
Plant Stress ◽  
Stress Protein ◽  
Protein Database

Conformational selection of the intrinsically disordered plant stress protein COR15A in response to solution osmolarity – an X-ray and light scattering study

2019 ◽  
Vol 21 (34) ◽  
pp. 18727-18740 ◽  
Author(s):  
Keyun Shou ◽  
Anne Bremer ◽  
Tobias Rindfleisch ◽  
Patrick Knox-Brown ◽  
Mitsuhiro Hirai ◽  
...  
Keyword(s):  
Light Scattering ◽  
Plant Stress ◽  
Stress Protein ◽  
Chloroplast Membranes ◽  
X Ray ◽  
Conformational Selection ◽  
Intrinsically Disordered ◽  
Scattering Study ◽  
Selection Of

The plant stress protein COR15A stabilizes chloroplast membranes during freezing.

Hierarchy of π-Stacking Determines the Conformational Preference of Bis-Squaraines

2020 ◽  
Author(s):  
Abhishek Singh ◽  
Reman K. Singh ◽  
G Naresh Patwari
Keyword(s):  
Hydrogen Bonding ◽  
Rational Design ◽  
Biological Molecules ◽  
Conformational Space ◽  
X Ray Crystallography ◽  
Simple Strategy ◽  
Induced Folding ◽  
Π Stacking ◽  
Varying Length ◽  
Dynamics Simulations

The rational design of conformationally controlled foldable modules can lead to a deeper insight into the conformational space of complex biological molecules where non-covalent interactions such as hydrogen bonding and π-stacking are known to play a pivotal role. Squaramides are known to have excellent hydrogen bonding capabilities and hence, are ideal molecules for designing foldable modules that can mimic the secondary structures of bio-molecules. The π-stacking induced folding of bis-squaraines tethered using aliphatic primary and secondary-diamine linkers of varying length is explored with a simple strategy of invoking small perturbations involving the length linkers and degree of substitution. Solution phase NMR investigations in combination with molecular dynamics simulations suggest that bis-squaraines predominantly exist as extended conformations. Structures elucidated by X-ray crystallography confirmed a variety of folded and extended secondary conformations including hairpin turns and 𝛽-sheets which are determined by the hierarchy of π-stacking relative to N–H···O hydrogen bonds.

Hierarchy of π-Stacking Determines the Conformational Preference of Bis-Squaraines

2020 ◽  
Author(s):  
Abhishek Singh ◽  
Reman K. Singh ◽  
G Naresh Patwari
Keyword(s):  
Hydrogen Bonding ◽  
Rational Design ◽  
Biological Molecules ◽  
Conformational Space ◽  
X Ray Crystallography ◽  
Simple Strategy ◽  
Induced Folding ◽  
Π Stacking ◽  
Varying Length ◽  
Dynamics Simulations

The rational design of conformationally controlled foldable modules can lead to a deeper insight into the conformational space of complex biological molecules where non-covalent interactions such as hydrogen bonding and π-stacking are known to play a pivotal role. Squaramides are known to have excellent hydrogen bonding capabilities and hence, are ideal molecules for designing foldable modules that can mimic the secondary structures of bio-molecules. The π-stacking induced folding of bis-squaraines tethered using aliphatic primary and secondary-diamine linkers of varying length is explored with a simple strategy of invoking small perturbations involving the length linkers and degree of substitution. Solution phase NMR investigations in combination with molecular dynamics simulations suggest that bis-squaraines predominantly exist as extended conformations. Structures elucidated by X-ray crystallography confirmed a variety of folded and extended secondary conformations including hairpin turns and 𝛽-sheets which are determined by the hierarchy of π-stacking relative to N–H···O hydrogen bonds.

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