Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins

FEBS Letters
J YaoP E Wright

Abstract

The intrinsic chemical shift dispersion for 15N, 1HN, 13C(alpha), 1H(alpha), 13C(beta) and 13CO resonances has been evaluated utilizing complete resonance assignment data for unfolded apomyoglobin, together with two other unfolded and five folded proteins, obtained from the literature. The dispersion of 13C(alpha), 1H(alpha), and 13C(beta) resonances for the unfolded proteins is poor, whereas the dispersion of 15N, 1HN and 13CO is much greater, reflecting the sensitivity of these nuclei to the nature of the neighboring amino acid in the primary sequence. By contrast, the dispersion of the 13C(alpha), 1H(alpha), and 13C(beta) nuclei are much greater in the folded proteins, reflecting the well-known dependence of the environments of these nuclei on secondary and tertiary structure. These differences in chemical shift dispersion dictate differences in strategies for resonance assignment in unfolded proteins compared with those most commonly used for folded proteins. Strategies utilizing the superior chemical shift dispersion of the 15N, 1HN and, in particular, the 13CO nuclei, are indicated for use with unfolded or partially folded proteins.

References

May 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·D NeriK Wüthrich
Nov 20, 1991·Journal of Molecular Biology·D S WishartF M Richards
Jul 5, 1988·Journal of Molecular Biology·Y V GrikoV P Kutyshenko
Jan 1, 1994·Methods in Enzymology·G M Clore, A M Gronenborn
Jan 1, 1994·Methods in Enzymology·D S Wishart, B D Sykes
Sep 27, 1994·Proceedings of the National Academy of Sciences of the United States of America·V L ArcusA R Fersht
Nov 1, 1995·Journal of Biomolecular NMR·P A JenningsP E Wright
Oct 15, 1996·Proceedings of the National Academy of Sciences of the United States of America·R W KriwackiP E Wright
Jan 1, 1996·Annual Review of Physical Chemistry·H J Dyson, P E Wright

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Citations

Jul 31, 1998·Protein Science : a Publication of the Protein Society·R GueroisA Sanson
Jun 27, 2007·Journal of Biomolecular NMR·Eszter Czinki, Attila G Császár
May 4, 2010·Journal of Biomolecular NMR·Sampo MäntylahtiPerttu Permi
Oct 12, 2012·Journal of Structural and Functional Genomics·Dinesh KumarRamakrishna V Hosur
Oct 23, 1998·Nature Structural Biology·P A Jennings
Apr 17, 2009·The Journal of Biological Chemistry·Laszlo L P HosszuAnthony R Clarke
Apr 24, 2001·Protein Science : a Publication of the Protein Society·Y BaiP E Wright
Jan 13, 2000·Protein Science : a Publication of the Protein Society·G A LazarT M Handel
Apr 22, 1999·Protein Science : a Publication of the Protein Society·E de AlbaM A Jiménez
Mar 30, 2000·Protein Science : a Publication of the Protein Society·S CavagneroP E Wright
Jan 11, 2001·Protein Science : a Publication of the Protein Society·C M SantiveriM A Jiménez
May 4, 2000·Protein Science : a Publication of the Protein Society·Y K MokG de Prat-Gay
May 11, 2010·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·David S LibichGeorge Harauz
Apr 5, 2014·Journal of Biomolecular NMR·David Pantoja-Uceda, Jorge Santoro
Oct 5, 2013·The Journal of Chemical Physics·Martin Gruebele, D Thirumalai
Apr 5, 2001·Journal of Molecular Biology·D EliezerG Browne
Mar 17, 2005·Proceedings of the National Academy of Sciences of the United States of America·Chiaki NishimuraPeter E Wright
May 13, 2014·Journal of Biomolecular NMR·Jakob Toudahl NielsenNiels Chr Nielsen
Jul 6, 2000·Proceedings of the National Academy of Sciences of the United States of America·B S RussellK L Bren
Feb 14, 2016·Biochimica Et Biophysica Acta·Mert ColpanAlla S Kostyukova
Nov 28, 2009·Journal of Virological Methods·Shaheen ShojaniaJoe D O'Neil
Mar 3, 2015·Scientific Reports·Akshay Kumar GangulyNeel Sarovar Bhavesh
Apr 7, 2006·Protein Science : a Publication of the Protein Society·Yoon-Hui Sung, David Eliezer
Feb 3, 2006·Protein Science : a Publication of the Protein Society·Preeti ChughaTerrence G Oas
Nov 10, 2012·Protein Science : a Publication of the Protein Society·Samantha B Nicholls, Jeanne A Hardy
Jan 14, 2010·The FEBS Journal·Anissa BoumlicGeorges Orfanoudakis
Jun 7, 2011·Journal of Molecular Biology·Chiaki NishimuraPeter E Wright
Apr 7, 2010·Journal of Molecular Biology·Stacy-Anne MorganG Andrew Woolley
Apr 9, 2008·FEBS Letters·H Jane DysonMaria A Martinez-Yamout
Apr 6, 2005·Methods in Enzymology·H Jane Dyson, Peter E Wright
Oct 13, 2011·Organic Letters·Martha G BomarAmit K Galande

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