Studied with the Relaxation Measurement of Mixed Zero- and Double-Quantum Coherences of CαH Systems

Abstract

Abstract:

More and more evidence indicates that the information on protein dynamics extracted from the “traditional” measurement of longitudinal, transverse and NOE cross relaxation rates is insufficient for a full description of the complex motions a protein may have, such as chemical and conformational exchanges or the interaction-induced dynamics changes. Extra dynamic information can be obtained from relaxation mechanism involving multi-quantum coherences. In this article, the effective relaxation rates of mixed zero- and double-quantum coherences of CαH systems in two proteins (one with ¹³C labeled and one natural abundant) have been measured with a modified pulse sequence. The trend of the relaxation rates with the change of the intervals between π pulses in CPMG period indicates the ubiquitous existence of exchange in the proteins. The temperature dependence of protein dynamics is shown with the measurement of effective transverse relaxation rates for three different temperatures. It is also found that the number of exchanging sites varies with type and location of the residue in a protein. Furthermore, quantitative analysis indicates that the effect of exchange on relaxation rate suggests that the presence of multi-site exchanges is common feature for proteins in solution, signifying that the exchange model currently used in description of protein exchange dynamics needs to be improved.

Key words: protein dynamics, relaxation, exchange, multi-quantum coherence, CPMG

CLC Number:

O482.53

Yan-Shi LIN , Ching-Hsia FANG, Shang-Wu DING. Studied with the Relaxation Measurement of Mixed Zero- and Double-Quantum Coherences of CαH Systems[J]. Chinese Journal of Magnetic Resonance, 2010, 27(3): 445-460.

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