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Default Three-dimensional structure and mimetic-membrane association of consensus 11-amino-acid motif from soybean lea3 protein.

Three-dimensional structure and mimetic-membrane association of consensus 11-amino-acid motif from soybean lea3 protein.

Related Articles Three-dimensional structure and mimetic-membrane association of consensus 11-amino-acid motif from soybean lea3 protein.

Biopolymers. 2012;98(1):59-66

Authors: Xue R, Liu Y, Zheng Y, Wu Y, Li X, Pei F, Ni J

Abstract
The occurrence of a highly conserved 11-mer repeating motif in the primary sequence is a major characteristic of group 3 late embryogenesis abundant (LEA3) proteins, which are strongly associated with abiotic stress tolerance of the plants. In this study, the three-dimensional structure, mimetic membrane association, and salt effect for consensus 11-mer motif from soybean PM2 protein (LEA3) were investigated in sodium dodecyl sulfate (SDS) micelles by NMR techniques. It was shown that the 11-mer motif was disordered in aqueous solution, but adopted an ?-helix in SDS micelles. NMR diffusion measurements demonstrated that the 11-mer motif was associated with SDS micelles. Paramagnetic quenching NMR experiments further revealed the orientation of the 11-mer motif with respect to the mimetic membrane: the ordered N-terminal segment was inserted into the mimetic membrane, and the disordered C-terminal segment was exposed to water. In addition, salt addition could not change the secondary structure of the 11-mer motif, but might slightly alter the relative spatial position of some N-terminal residue atoms. These results implied that the 11-mer motif would take an important role in structural plasticity and membrane stabilization for LEA3 proteins. © 2011 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 59-66, 2012.


PMID: 23325560 [PubMed - in process]



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