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
Agnieszka Lewandowska
Laboratory of Biopolymer Structure, Intercollegiate Faculty of Biotechnology, University of Gdańsk, Medical University of Gdańsk, Kładki 24, 80-822 Gdańsk, Poland
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Agnieszka Lewandowska was formerly known as Skwierawska.
Search for more papers by this authorStanisław Ołdziej
Laboratory of Biopolymer Structure, Intercollegiate Faculty of Biotechnology, University of Gdańsk, Medical University of Gdańsk, Kładki 24, 80-822 Gdańsk, Poland
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Search for more papers by this authorAdam Liwo
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Faculty of Chemistry, University of Gdańsk, Sobieskiego 18, 80-952 Gdańsk, Poland
Search for more papers by this authorCorresponding Author
Harold A. Scheraga
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301===Search for more papers by this authorAgnieszka Lewandowska
Laboratory of Biopolymer Structure, Intercollegiate Faculty of Biotechnology, University of Gdańsk, Medical University of Gdańsk, Kładki 24, 80-822 Gdańsk, Poland
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Agnieszka Lewandowska was formerly known as Skwierawska.
Search for more papers by this authorStanisław Ołdziej
Laboratory of Biopolymer Structure, Intercollegiate Faculty of Biotechnology, University of Gdańsk, Medical University of Gdańsk, Kładki 24, 80-822 Gdańsk, Poland
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Search for more papers by this authorAdam Liwo
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Faculty of Chemistry, University of Gdańsk, Sobieskiego 18, 80-952 Gdańsk, Poland
Search for more papers by this authorCorresponding Author
Harold A. Scheraga
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301===Search for more papers by this authorAbstract
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. © 2009 Wiley-Liss, Inc.
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