Biopolym. Cell. 2006; 22(3):225-230.
http://dx.doi.org/10.7124/bc.000734
Molecular Biophysics
Theoretical evaluation of the peptide chain segmental mobility in the molecule of human serum albumin
1Shchechkin I. E., 1Hushcha T. O.
  1. Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine
    1, Murmans'ka Str., Kyiv, Ukraine, 02094

Abstract

The method for evaluation of mobility of peptide chain fragments in globular proteins is proposed. The method is based on the analysis of both the protein 3D structure friability and the values of non valent interactions between protein chain residues. The analysis is performed for a single protein conformation taken from X-ray structural data. The application of the proposed method to the molecule of human serum albumin has shown that the best mobility may be expected for the terminal chain segments (in the range of 33–137 and 500–582 residues), as well as for the segments located in the middle of the chain (257–304 residues). The obtained results may be used for selection of a mobility model while studying albumins dynamics.
Keywords: human serum albumin, conformational mobility, peptide chain, 3D structure friability
Full text: (PDF, in Russian)

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