TROSY-based NMR experiments for the study of macromolecular dynamics and hydrogen bonding.

Guang Zhu; Youlin Xia; Donghai Lin; Xiaolian Gao

TROSY-based NMR experiments for the study of macromolecular dynamics and hydrogen bonding.

Guang Zhu, Youlin Xia, Donghai Lin, Xiaolian Gao

Minnesota NMR Center

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Transverse relaxation-optimized spectroscopy (TROSY)-based nuclear magnetic resonance (NMR) experiments can be exploited to obtain chemical shift assignment and values of J-coupling constants, residual dipolar couplings, and nuclear Overhauser effects (NOEs) for structural studies of proteins, as discussed in Chapter 5. Furthermore, the application of TROSY-based NMR experiments can be extended to the measurements of molecule dynamics, amide proton exchange rates, and hydrogen bonds. This chapter describes these experiments.

Original language	English (US)
Pages (from-to)	161-184
Number of pages	24
Journal	Methods in molecular biology (Clifton, N.J.)
Volume	278
State	Published - 2004

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abstract = "Transverse relaxation-optimized spectroscopy (TROSY)-based nuclear magnetic resonance (NMR) experiments can be exploited to obtain chemical shift assignment and values of J-coupling constants, residual dipolar couplings, and nuclear Overhauser effects (NOEs) for structural studies of proteins, as discussed in Chapter 5. Furthermore, the application of TROSY-based NMR experiments can be extended to the measurements of molecule dynamics, amide proton exchange rates, and hydrogen bonds. This chapter describes these experiments.",

author = "Guang Zhu and Youlin Xia and Donghai Lin and Xiaolian Gao",

year = "2004",

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T1 - TROSY-based NMR experiments for the study of macromolecular dynamics and hydrogen bonding.

AU - Zhu, Guang

AU - Xia, Youlin

AU - Lin, Donghai

AU - Gao, Xiaolian

PY - 2004

Y1 - 2004

N2 - Transverse relaxation-optimized spectroscopy (TROSY)-based nuclear magnetic resonance (NMR) experiments can be exploited to obtain chemical shift assignment and values of J-coupling constants, residual dipolar couplings, and nuclear Overhauser effects (NOEs) for structural studies of proteins, as discussed in Chapter 5. Furthermore, the application of TROSY-based NMR experiments can be extended to the measurements of molecule dynamics, amide proton exchange rates, and hydrogen bonds. This chapter describes these experiments.

AB - Transverse relaxation-optimized spectroscopy (TROSY)-based nuclear magnetic resonance (NMR) experiments can be exploited to obtain chemical shift assignment and values of J-coupling constants, residual dipolar couplings, and nuclear Overhauser effects (NOEs) for structural studies of proteins, as discussed in Chapter 5. Furthermore, the application of TROSY-based NMR experiments can be extended to the measurements of molecule dynamics, amide proton exchange rates, and hydrogen bonds. This chapter describes these experiments.

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JO - Methods in Molecular Biology

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TROSY-based NMR experiments for the study of macromolecular dynamics and hydrogen bonding.

Abstract

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