Abstract:Multiple quantum relaxation in proteins reveals unexpected relationships between correlated or anti-correlated conformational backbone dynamics in R-helices or -sheets. The contributions of confor-mational exchange to the relaxation rates of C′N coherences (i.e., double- and zero-quantum coherences involving backbone carbonyl 13 C′ and neighboring amide 15 N nuclei) depend on the kinetics of slow exchange processes, as well as on the populations of the conformations and chemical shift differences of 13 C′ and 15 N nuclei. The relaxation rates of C′N coherences, which reflect concerted fluctuations due to slow chemical shift modulations (CSMs), were determined by direct 13 C detection in diamagnetic and paramagnetic proteins. In well-folded proteins such as lanthanide-substituted calbindin (CaLnCb), copper,zinc superoxide dismutase (Cu,Zn SOD), and matrix metalloproteinase (MMP12), slow conformational exchange occurs along the entire backbone. Our observations demonstrate that relaxation rates of C′N coherences arising from slow backbone dynamics have positive signs (characteristic of correlated fluctuations) in -sheets and negative signs (characteristic of anti-correlated fluctuations) in R-helices. This extends the prospects of structure -dynamics relationships to slow time scales that are relevant for protein function and enzymatic activity.

Towards structural dynamics: protein motions viewed by chemical shift modulations and direct detection of C’N multiple-quantum relaxation / M.Mori; F.Kateb; G.Bodenhausen; M.Piccioli;D.Abergel. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 132(2010), pp. 3594-3600. [10.1021/ja9103556]

Towards structural dynamics: protein motions viewed by chemical shift modulations and direct detection of C’N multiple-quantum relaxation

MORI, MIRKO;PICCIOLI, MARIO;
2010

Abstract

Abstract:Multiple quantum relaxation in proteins reveals unexpected relationships between correlated or anti-correlated conformational backbone dynamics in R-helices or -sheets. The contributions of confor-mational exchange to the relaxation rates of C′N coherences (i.e., double- and zero-quantum coherences involving backbone carbonyl 13 C′ and neighboring amide 15 N nuclei) depend on the kinetics of slow exchange processes, as well as on the populations of the conformations and chemical shift differences of 13 C′ and 15 N nuclei. The relaxation rates of C′N coherences, which reflect concerted fluctuations due to slow chemical shift modulations (CSMs), were determined by direct 13 C detection in diamagnetic and paramagnetic proteins. In well-folded proteins such as lanthanide-substituted calbindin (CaLnCb), copper,zinc superoxide dismutase (Cu,Zn SOD), and matrix metalloproteinase (MMP12), slow conformational exchange occurs along the entire backbone. Our observations demonstrate that relaxation rates of C′N coherences arising from slow backbone dynamics have positive signs (characteristic of correlated fluctuations) in -sheets and negative signs (characteristic of anti-correlated fluctuations) in R-helices. This extends the prospects of structure -dynamics relationships to slow time scales that are relevant for protein function and enzymatic activity.
132
3594
3600
M.Mori; F.Kateb; G.Bodenhausen; M.Piccioli;D.Abergel
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2158/371152
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