Amino acid intrinsic alpha-helical propensities III: positional dependence at several positions of C terminus

Protein Science : a Publication of the Protein Society
M PetukhovL Serrano

Abstract

In this study, we have analyzed experimentally the helical intrinsic propensities of non-charged and non-aromatic residues at different C-terminal positions (C1, C2, C3) of an Ala-based peptide. The effect was found to be complex, resulting in extra stabilization or destabilization, depending on guest amino acid and position under consideration. Polar (Ser, Thr, Cys, Asn, and Gln) amino acids and Gly were found to have significantly larger helical propensities at several C-terminal positions compared with the alpha-helix center (-1.0 kcal/mole in some cases). Some of the nonpolar residues, especially beta-branched ones (Val and Ile) are significantly more favorable at position C3 (-0.3 to -0.4 kcal/mole), although having minor differences at other C-terminal positions compared with the alpha-helix center. Leu has moderate (-0.1 to -0.2 kcal/mole) stabilization effects at position C2 and C3, whereas being relatively neutral at C1. Finally, Met was found to be unfavorable at C1 and C2 ( +0.2 kcal/mole) and favorable at C3 (-0.2 kcal/mole). Thus, significant differences found between the intrinsic helical propensities at the C-terminal positions and those in the alpha-helix center must be accounted for in helix/coil transition the...Continue Reading

References

May 25, 1977·Journal of Molecular Biology·F C BernsteinM Tasumi
Feb 1, 1992·Protein Science : a Publication of the Protein Society·L Wesson, D Eisenberg
Jun 13, 1991·Nature·A ChakrabarttyR L Baldwin
Mar 1, 1990·Journal of Molecular Graphics·G Vriend
Nov 1, 1989·Analytical Biochemistry·S C Gill, P H von Hippel
Feb 1, 1989·Journal of Biomolecular Structure & Dynamics·A K Mazur, R A Abagyan
Feb 1, 1989·Journal of Biomolecular Structure & Dynamics·R A Abagyan, A K Mazur
Jun 17, 1988·Science·J S Richardson, D C Richardson
Aug 4, 1995·Journal of Molecular Biology·A R Viguera, L Serrano
Jun 1, 1994·Nature Structural Biology·V Muñoz, L Serrano
Jul 1, 1995·Nature Structural Biology·M B SwindellsJ M Thornton
Jul 1, 1995·Protein Science : a Publication of the Protein Society·A J Doig, R L Baldwin
May 1, 1994·Protein Science : a Publication of the Protein Society·A ChakrabarttyR L Baldwin
Jun 1, 1994·Proteins·T P Creamer, G D Rose
Aug 3, 1993·Biochemistry·E T Harper, G D Rose
Jun 11, 1993·Science·M BlaberB W Matthews
Feb 12, 1998·Journal of Molecular Biology·J Prieto, L Serrano
Mar 26, 1998·Protein Science : a Publication of the Protein Society·R Aurora, G D Rose
May 26, 1998·Journal of Molecular Biology·M PetukhovL Serrano
Jun 19, 1998·Current Opinion in Structural Biology·A Warshel, A Papazyan
Aug 4, 1999·Proceedings of the National Academy of Sciences of the United States of America·A G Street, S L Mayo
Nov 5, 1999·Protein Science : a Publication of the Protein Society·M PetukhovL Serrano
May 4, 2000·Protein Science : a Publication of the Protein Society·J K SunA J Doig
May 10, 2001·Protein Science : a Publication of the Protein Society·D A CochranA J Doig
Jun 23, 2001·Protein Science : a Publication of the Protein Society·D A Cochran, A J Doig
Sep 6, 2001·Proceedings of the National Academy of Sciences of the United States of America·S T ThomasG I Makhatadze

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Citations

Feb 9, 2006·Chemical Reviews·Patrick J O'Brien
Oct 6, 2010·BMC Structural Biology·Nicholus Bhattacharjee, Parbati Biswas
Aug 15, 2009·Computational Biology and Chemistry·Steinar Thorvaldsen, Elinor Ytterstad
Dec 21, 2005·Journal of Molecular Biology·J López-LlanoJ Sancho
Jul 2, 2016·Journal of Biomolecular Structure & Dynamics·Alessandra ApicellaChristopher J G Plummer
Jul 17, 2012·The Journal of Physical Chemistry. B·Simon Mathieu, Georges Trinquier
Oct 24, 2003·Protein Science : a Publication of the Protein Society·Bosco K HoRobert Brasseur
Jan 18, 2017·Scientific Reports·Jason M CramerDavid C Williams
May 23, 2003·Protein Science : a Publication of the Protein Society·Dmitri N ErmolenkoGeorge I Makhatadze
Jul 27, 2007·Proteins·Nuno A FonsecaA L Magalhães
Feb 18, 2009·Journal of Peptide Science : an Official Publication of the European Peptide Society·Michael PetukhovNoboru Yumoto
Jan 30, 2021·Protein Science : a Publication of the Protein Society·Tatjana ŠkrbićJayanth R Banavar
Apr 7, 2005·Journal of the American Chemical Society·Teuku M Iqbalsyah, Andrew J Doig
Mar 9, 2005·Archives of Biochemistry and Biophysics·Wiliam C B RegisCarlos H I Ramos
Oct 12, 2010·Biochemistry·Richard P ChengOlivia Barrett
Aug 15, 2002·Journal of the American Chemical Society·Sara M ButterfieldMarcey L Waters

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