PMID: 7088178Jul 15, 1982Paper

Conformation of terminal regions in proteins

Nature
J M Thornton, B L Chakauya

Abstract

A carboxy-terminal helix has been observed in many proteins, suggesting that these helices confer an advantage, perhaps by providing protection against carboxypeptidase activity. To determine whether the conformational preferences of the amino- and carboxy-terminal regions are significantly different from each other and from the rest of the protein, we have analysed all proteins of known structure. We report here that the resulting distribution of the helical, beta-strand and coil conformations is significantly different for the amino- and carboxy-terminals; the former preferentially adopts an extended beta-strand while the latter is usually helical. The observed difference derives from the alpha/beta proteins, in which the helix and strand alternate along the sequence, suggesting that the origin of this preference lies, not in protection against degradation, but in the special structural topology of alpha/beta proteins and the beta alpha unit.

References

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Citations

Jun 8, 2001·Progress in Biophysics and Molecular Biology·P Chakrabarti, D Pal
Jan 24, 2007·Bioinformatics·Etai Jacob, Ron Unger
Dec 3, 2003·Reviews in the Neurosciences·R Lalonde, C Strazielle
Jan 20, 2005·Proceedings of the National Academy of Sciences of the United States of America·Mallela M G Krishna, S Walter Englander
Oct 8, 1998·The Journal of Cell Biology·N Hirokawa, S Takeda
Nov 11, 2005·Proteins·Alessandro Laio, Cristian Micheletti
Jun 25, 1983·Journal of Molecular Biology·J M Thornton, B L Sibanda
Nov 16, 2013·Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics·M LundgrenAntti J Niemi

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