Mechanism of formation of the C‐terminal β‐hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. III. Dynamics of long‐range hydrophobic interactions
- 11 September 2009
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 78 (3), 723-737
- https://doi.org/10.1002/prot.22605
Abstract
A 20‐residue peptide, IG(42–61), derived from the C‐terminal β‐hairpin of the B3 domain of the immunoglobulin binding protein G from Streptoccocus was studied using circular dichroism, nuclear magnetic resonance (NMR) spectroscopy at various temperatures and by differential scanning calorimetry (DSC). Unlike other related peptides studied so far, this peptide displays two heat capacity peaks in DSC measurements (at a scanning rate of 1.5 deg/min at a peptide concentration of 0.07 mM), which suggests a three‐state folding/unfolding process. The results from DSC and NMR measurements suggest the formation of a dynamic network of hydrophobic interactions stabilizing the structure, which resembles a β‐hairpin shape over a wide range of temperatures (283–313 K). Our results show that IG (42–61) possesses a well‐organized three‐dimensional structure stabilized by long‐range hydrophobic interactions (Tyr50 ··· Phe57 and Trp48 ··· Val59) at T = 283 K and (Trp48 ··· Val59) at 305 and 313 K. The mechanism of β‐hairpin folding and unfolding, as well as the influence of peptide length on its conformational properties, are also discussed. Proteins 2010.Keywords
This publication has 71 references indexed in Scilit:
- Mechanism of formation of the C‐terminal β‐hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. II. Interplay of local backbone conformational dynamics and long‐range hydrophobic interactions in hairpin formationProteins-Structure Function and Bioinformatics, 2009
- Mechanism of formation of the C‐terminal β‐hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. I. Importance of hydrophobic interactions in stabilization of β‐hairpin structureProteins-Structure Function and Bioinformatics, 2008
- Conformational studies of the C-terminal 16-amino-acid-residue fragment of the B3 domain of the immunoglobulin binding protein G fromStreptococcusBiopolymers, 2008
- Conformational studies of the α‐helical 28–43 fragment of the B3 domain of the immunoglobulin binding protein G from StreptococcusBiopolymers, 2008
- Folding Pathway of the B1 Domain of Protein G Explored by Multiscale ModelingBiophysical Journal, 2008
- The role of hydrophobic interactions in initiation and propagation of protein foldingProceedings of the National Academy of Sciences, 2006
- Torsion angle dynamics for NMR structure calculation with the new program DyanaJournal of Molecular Biology, 1997
- Structural analysis of peptides encompassing all α-helices of three α/β parallel proteins: Che-Y, flavodoxin and P21-Ras: Implications for α-Helix stability and the folding of α/β parallel proteinsJournal of Molecular Biology, 1995
- The Third IgG-Binding Domain from Streptococcal Protein GJournal of Molecular Biology, 1994
- Time-dependent distance restraints in molecular dynamics simulationsChemical Physics Letters, 1989