Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation

Mengjun Xue; Ryo Kitahara; Yuichi Yoshimura; Frans A A Mulder

doi:10.1016/j.bbrc.2016.08.092

Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation

Mengjun Xue, Ryo Kitahara, Yuichi Yoshimura, Frans A A Mulder

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

3 Citations (Scopus)

Abstract

Hydrogen exchange (HX) NMR spectroscopy is widely used for monitoring structure, stability and dynamics of proteins at the level of individual residues. The stochastic replacement of protons by deuterons typically leads to an exponential decrease of the NMR signals. However, an unusual signal increase was observed in HX of several amides for T4 lysozyme L99A. This effect can be attributed to peak sharpening as a result of reduced dipolar relaxation from proximal amide protons that experience more rapid hydrogen/deuterium (H/D) exchange. The behavior was specifically observed at the termini of secondary structure elements, where large differences in protection against H/D exchange are observed. This effect is expected to be more widespread in NMR HX studies, and is important for the accurate determination of protection factors.

Original language	English
Journal	Biochemical and Biophysical Research Communications
Volume	478
Issue	3
Pages (from-to)	1185-1188
Number of pages	4
ISSN	0006-291X
DOIs	https://doi.org/10.1016/j.bbrc.2016.08.092
Publication status	Published - 2016

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10.1016/j.bbrc.2016.08.092

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title = "Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation",

abstract = "Hydrogen exchange (HX) NMR spectroscopy is widely used for monitoring structure, stability and dynamics of proteins at the level of individual residues. The stochastic replacement of protons by deuterons typically leads to an exponential decrease of the NMR signals. However, an unusual signal increase was observed in HX of several amides for T4 lysozyme L99A. This effect can be attributed to peak sharpening as a result of reduced dipolar relaxation from proximal amide protons that experience more rapid hydrogen/deuterium (H/D) exchange. The behavior was specifically observed at the termini of secondary structure elements, where large differences in protection against H/D exchange are observed. This effect is expected to be more widespread in NMR HX studies, and is important for the accurate determination of protection factors.",

author = "Mengjun Xue and Ryo Kitahara and Yuichi Yoshimura and Mulder, {Frans A A}",

year = "2016",

doi = "10.1016/j.bbrc.2016.08.092",

language = "English",

volume = "478",

pages = "1185--1188",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

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Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation. / Xue, Mengjun; Kitahara, Ryo; Yoshimura, Yuichi et al.
In: Biochemical and Biophysical Research Communications, Vol. 478, No. 3, 2016, p. 1185-1188.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation

AU - Xue, Mengjun

AU - Kitahara, Ryo

AU - Yoshimura, Yuichi

AU - Mulder, Frans A A

PY - 2016

Y1 - 2016

N2 - Hydrogen exchange (HX) NMR spectroscopy is widely used for monitoring structure, stability and dynamics of proteins at the level of individual residues. The stochastic replacement of protons by deuterons typically leads to an exponential decrease of the NMR signals. However, an unusual signal increase was observed in HX of several amides for T4 lysozyme L99A. This effect can be attributed to peak sharpening as a result of reduced dipolar relaxation from proximal amide protons that experience more rapid hydrogen/deuterium (H/D) exchange. The behavior was specifically observed at the termini of secondary structure elements, where large differences in protection against H/D exchange are observed. This effect is expected to be more widespread in NMR HX studies, and is important for the accurate determination of protection factors.

AB - Hydrogen exchange (HX) NMR spectroscopy is widely used for monitoring structure, stability and dynamics of proteins at the level of individual residues. The stochastic replacement of protons by deuterons typically leads to an exponential decrease of the NMR signals. However, an unusual signal increase was observed in HX of several amides for T4 lysozyme L99A. This effect can be attributed to peak sharpening as a result of reduced dipolar relaxation from proximal amide protons that experience more rapid hydrogen/deuterium (H/D) exchange. The behavior was specifically observed at the termini of secondary structure elements, where large differences in protection against H/D exchange are observed. This effect is expected to be more widespread in NMR HX studies, and is important for the accurate determination of protection factors.

U2 - 10.1016/j.bbrc.2016.08.092

DO - 10.1016/j.bbrc.2016.08.092

M3 - Journal article

C2 - 27544032

SN - 0006-291X

VL - 478

SP - 1185

EP - 1188

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation

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