beta 2-Strand of salivary S cystatins: A "chemeleon sequence"

Cristiana Carelli Alinovi, A Vitali, Mc De Rosa, R. Petruzzelli

Risultato della ricerca: Contributo in rivistaArticolo in rivista

Abstract

Secondary structure prediction of salivary cystatins S, SA, and SN carried out by several methods label the 39–58 sequence (β2-strand) as predominantly α-helical. The helical propensity of a peptide corresponding to β2-strand of salivary SA cystatin analyzed by CD display high helical propensity in aqueous solution, whereas peptides matching the β2-strand amino acid sequence of cystatins S and SN, display random coil conformation in aqueous solution but acquire α-helical conformation in the presence of trifluoroethanol (TFE). Moreover molecular dynamics simulation performed on the homology modeling of cystatin SA constructed on the basis of recently determined three-dimensional structure of salivary cystatin D, suggests that cystatin SA does not significantly deviate from the starting structure over the course of the simulation. The results obtained indicate that the β2-strand of salivary S cystatins has high helical propensity when isolated from native protein and acquire the final β structure by interaction with the rest of the polypeptide chain.
Lingua originaleEnglish
pagine (da-a)47-51
Numero di pagine5
RivistaBiochemical and Biophysical Research Communications
Volume387
DOI
Stato di pubblicazionePubblicato - 2009

Keywords

  • CD
  • Capping box
  • Folding
  • Molecular modeling
  • Peptide
  • Salivary cystatins
  • α-Helix
  • β-Strand

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