Wioletta Żmudzińska

University of Gdansk, Danzig, Pomeranian Voivodeship, Poland

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Publications (2)7.21 Total impact

  • Biophysical Journal 01/2015; 108(2):158a. DOI:10.1016/j.bpj.2014.11.870 · 3.83 Impact Factor
  • Anna Hałabis, Wioletta Żmudzińska, Adam Liwo, Stanisław Ołdziej
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    ABSTRACT: The folding temperature of the trp-cage mini-protein was determined to be in the range 311-317 K depending on the method used. Our study is focused on determining the structure and dynamics of the polypeptide chain close to its unfolding or melting temperature. At T = 305 K, Trp6-Arg16 and Trp6-Pro12 long-range interactions are observed, and at T = 313 K, only the Trp6-Arg16 interactions remain, while all of mentioned interactions are observed in the native state of the protein. Partial (at T = 305 K) and complete (at T = 313 K) melting of the N-terminal α-helix is observed, manifested by the appearance of minor sets of signals in NMR spectra. Our key findings are: (i) conformational phase transition (melting point) could be described as a cooperative breaking of the Trp6-Pro12 long-range hydrophobic interaction and the melting of the N-terminal α-helix; (ii) many ROE signals corresponding to local or short-range interactions vanish rapidly with temperature increase; however, long-range interaction such as Trp6-Arg16 remains until 313 K. The presence of the native long-range interaction at 313 K makes that conformational ensemble resemble a very diffuse native state structure, but it is not a simple mixture of the folded and unfolded states, as could be expected on the basis of the common two-state folding mechanism.
    The Journal of Physical Chemistry B 04/2012; 116(23):6898-907. DOI:10.1021/jp212630y · 3.38 Impact Factor