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J Biomol Struct Dyn. 2014;32(2):257-72. doi: 10.1080/07391102.2012.762724. Epub 2013 Mar 25.

Dancing retro: solution structure and micelle interactions of the retro-SH3-domain, retro-SHH-'Bergerac'.

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1
a Institute of Theoretical and Experimental Biophysics of Russian Academy of Science , Pushchino , Moscow Region , 142290 , Russia .

Abstract

A protein with the reversed direction of its polypeptide chain, retro-SHH, was analyzed by several spectroscopic techniques including circular dichroism and high-resolution NMR to understand its solution structure and structural consequences of interaction with the micelles formed by the zwitterionic detergent dodecylphosphocholine (DPC). This analysis revealed that retro-SHH does not contain rigid 3-D structure, but is characterized by the presence of residual secondary structure. Intriguingly, interaction with the DPC micelles affected the structures of SHH and retro-SHH very differently. In fact, micelles induce pronounced folding of retro-SHH, whereas micelle-bound SHH was noticeably disordered. Finally, we performed a disorder prediction with the PONDR-FIT algorithm and discovered that the reversal of the chain direction almost does not affect the propensity of a polypeptide for intrinsic disorder, since the disorder plot for retro-SHH was almost a mirror image of that for the normal SHH.

PMID:
23527530
DOI:
10.1080/07391102.2012.762724
[Indexed for MEDLINE]

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