Literature DB >> 12397998

Sonication induced sheet formation at the air-water interface.

K S Satheeshkumar1, R Jayakumar.   

Abstract

A hydrophobic pentadecapeptide, AGAAAA-GAVVGGLGG (1), part of the prion sequence PrP (106-127), on fresh aqueous dissolution takes a mixture of random and sheet conformations which forms a stable monolayer with a high beta-sheet content when compressed at the air-water interface. This also develops into a kinetically stabilized beta-sheet structure on sonication.

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Year:  2002        PMID： 12397998     DOI： 10.1039/b206886a

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN： 1359-7345            Impact factor:   6.222


  4 in total

1.  Sonication of proteins causes formation of aggregates that resemble amyloid.

Authors:  Peter B Stathopulos; Guenter A Scholz; Young-Mi Hwang; Jessica A O Rumfeldt; James R Lepock; Elizabeth M Meiering
Journal:  Protein Sci       Date:  2004-09-30       Impact factor: 6.725

2.  Isolation of biologically active nanomaterial (inclusion bodies) from bacterial cells.

Authors:  Spela Peternel; Radovan Komel
Journal:  Microb Cell Fact       Date:  2010-09-10       Impact factor: 5.328

3.  Surfactant-induced conformational transition of amyloid beta-peptide.

Authors:  N Sureshbabu; R Kirubagaran; R Jayakumar
Journal:  Eur Biophys J       Date:  2008-11-13       Impact factor: 1.733

4.  Prion protein self-peptides modulate prion interactions and conversion.

Authors:  Alan Rigter; Jan Priem; Drophatie Timmers-Parohi; Jan P M Langeveld; Fred G van Zijderveld; Alex Bossers
Journal:  BMC Biochem       Date:  2009-11-30       Impact factor: 4.059
  4 in total

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