title: Dancing retro: solution structure and micelle interactions of the retro-SH3-domain, retro-SHH-'Bergerac'.
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.
authors.affiliation: a Institute of Theoretical and Experimental Biophysics of Russian Academy of Science , Pushchino , Moscow Region , 142290 , Russia .
authors.forename: Victor P
authors.initials: VP
authors.lastname: Kutyshenko
authors.forename: Dmitry A
authors.initials: DA
authors.lastname: Prokhorov
authors.forename: Nikolaj V
authors.initials: NV
authors.lastname: Molochkov
authors.forename: Mars G
authors.initials: MG
authors.lastname: Sharapov
authors.forename: Igor
authors.initials: I
authors.lastname: Kolesnikov
authors.forename: Vladimir N
authors.initials: VN
authors.lastname: Uversky
mesh_terms: D000595:Amino Acid Sequence; D050976:Basic-Leucine Zipper Transcription Factors / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D002942:Circular Dichroism; D008823:Micelles; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry; D010767:Phosphorylcholine / Q000031:analogs & derivatives / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012996:Solutions; D013329:Structure-Activity Relationship; D018909:src Homology Domains
chemical_list: D050976:Basic-Leucine Zipper Transcription Factors; D008823:Micelles; D010455:Peptides; D012996:Solutions; D010767:Phosphorylcholine; C028810:dodecylphosphocholine