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Default Fast hydrogen exchange affects (15)N relaxation measurements in intrinsically disordered proteins.

Fast hydrogen exchange affects (15)N relaxation measurements in intrinsically disordered proteins.

Related Articles Fast hydrogen exchange affects (15)N relaxation measurements in intrinsically disordered proteins.

J Biomol NMR. 2013 Jan 12;

Authors: Kim S, Wu KP, Baum J

Abstract
Unprotected amide protons can undergo fast hydrogen exchange (HX) with protons from the solvent. Generally, NMR experiments using the out-and-back coherence transfer with amide proton detection are affected by fast HX and result in reduced signal intensity. When one of these experiments, (1)H-(15)N HSQC, is used to measure the (15)N transverse relaxation rate (R(2)), the measured R(2) rate is convoluted with the HX rate (k(HX)) and has higher apparent R(2) values. Since the (15)N R(2) measurement is important for analyzing protein backbone dynamics, the HX effect on the R(2) measurement is investigated and described here by multi-exponential signal decay. We demonstrate these effects by performing (15)N R (2) (CPMG) experiments on ?-synuclein, an intrinsically disordered protein, in which the amide protons are exposed to solvent. We show that the HX effect on R (2) (CPMG) can be extracted by the derived equation. In conclusion, the HX effect may be pulse sequence specific and results from various sources including the J coupling evolution, the change of steady state water proton magnetization, and the D(2)O content in the sample. To avoid the HX effect on the analysis of relaxation data of unprotected amides, it is suggested that NMR experimental conditions insensitive to the HX should be considered or that intrinsic R (2) (CPMG) values be obtained by methods described herein.


PMID: 23314729 [PubMed - as supplied by publisher]



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