Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant.
We perform a detailed comparison of fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin headpiece C-terminal domain (DHP) and its S74E mutant (DHPS74E). Carbonyl dynamics is probed via auto-correlated longitudinal rates and transverse C'/C'-C(alpha) CSA/dipolar and C'/C'-N CSA/dipolar cross-correlated rates, while (15)N data are taken from a previous study. Resulting values of effective order parameters and internal correlation times support the conclusion that C' relaxation reports on a different subset of fast motions compared to those probed at N-H bond vectors in the same peptide planes. (13)C' order parameters are on the average 0.08 lower than (15)N order parameters with the exception of the flexible loop region in DHP. The reduction of mobility in the loop region upon the S74E mutation can be seen from the (15)N order parameters but not from the (13)C order parameters. Internal correlation times at (13)C' sites are on the average an order of magnitude longer than those at (15)N sites for the well-structured C-terminal subdomains, while the more flexible N-terminal subdomains have more comparable average internal correlation times.
Vugmeyster
Liliya
L
Department of Chemistry and Environment and Natural Resources Institute, University of Alaska at Anchorage, 3211 Providence Drive, Anchorage, AK 99508, USA. aflv@uaa.alaska.edu
Ostrovsky
Dmitry
D
Li
Ying
Y
D001798:Blood Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002247:Carbon Isotopes / Q000737:chemistry; D006801:Humans; D008840:Microfilament Proteins; D008958:Models, Molecular; D009154:Mutation; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D001798:Blood Proteins; D002247:Carbon Isotopes; C044805:DMTN protein, human; D008840:Microfilament Proteins; D009587:Nitrogen Isotopes; D010750:Phosphoproteins
Biochemistry. 2002 Feb 26;41(8):2655-66
11851412
Biochemistry. 2006 Mar 21;45(11):3653-63
16533048
J Biomol NMR. 1997 Jan;9(1):63-78
20683761
Methods Enzymol. 2007;423:149-65
17609130
J Chem Phys. 2007 Apr 7;126(13):134508
17430048
J Mol Biol. 1998 Mar 13;276(5):939-54
9566198
J Biomol NMR. 1995 Nov;6(3):277-93
8520220
Nature. 2005 Nov 3;438(7064):117-21
16267559
Chemphyschem. 2004 Jun 21;5(6):807-14
15253308
J Am Chem Soc. 2001 Jun 27;123(25):6118-26
11414846
J Magn Reson. 1998 Feb;130(2):346-51
9500898
Biochemistry. 1994 May 17;33(19):5984-6003
7514039
J Am Chem Soc. 2001 Apr 4;123(13):3055-63
11457016
Biophys J. 2008 Dec 15;95(12):5941-50
18820237
J Biomol NMR. 2003 Jul;26(3):203-13
12766418
Science. 2006 Apr 14;312(5771):224-8
16614210
J Magn Reson. 2011 Dec;213(2):423-41
22152361
Eur J Biochem. 1994 Feb 1;219(3):887-96
8112340
Chem Rev. 2004 Aug;104(8):3623-40
15303831
J Mol Biol. 1995 Feb 10;246(1):144-63
7531772
J Am Chem Soc. 2003 Jul 16;125(28):8639-43
12848571
J Am Chem Soc. 2005 Apr 27;127(16):6062-8
15839707
J Am Chem Soc. 2005 Jan 26;127(3):828-9
15656608
J Mol Graph. 1996 Feb;14(1):51-5, 29-32
8744573
J Biomol NMR. 2009 Jan;43(1):39-50
19030997
J Am Chem Soc. 2004 Sep 22;126(37):11424-5
15366873
Magn Reson Chem. 2007 Feb;45(2):175-8
17154329
Structure. 2006 Feb;14(2):379-87
16472756
J Biol Chem. 2004 Feb 27;279(9):7909-16
14660664
Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):16984-9
16278300
J Magn Reson. 2005 May;174(1):43-53
15809171
Biochim Biophys Acta. 1998 Jul 9;1398(3):382-6
9655941
J Am Chem Soc. 2003 Jul 30;125(30):9179-91
15369375
J Biomol NMR. 2006 Oct;36(2):79-102
17013680
J Am Chem Soc. 2003 Jul 9;125(27):8400-4
12837113
J Biomol NMR. 2003 Apr;25(4):265-80
12766390