Longitudinal and transverse 1H-15N dipolar/15N chemical shift anisotropy relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules

Christopher (Chris) Kroenke, J. Patrick Loria, Larry K. Lee, Mark Rance, Arthur G. Palmer

Research output: Contribution to journalArticle

220 Citations (Scopus)

Abstract

High-resolution proton-detected heteronuclear correlation NMR spectroscopy allows the measurement of 15N spin relaxation rates at multiple sites throughout a biological macromolecule. The rate constants are determined by stochastic internal motions on time scales of picoseconds to nanoseconds, overall molecular rotational diffusion on time scales of nanoseconds, and chemical exchange rates on time scales of microseconds to milliseconds. A new method has been developed for distinguishing the contributions of chemical exchange from the contributions due to anisotropic rotational diffusion by measuring both longitudinal and transverse interference between the 1H-15N dipolar and 15N chemical shift anisotropy interactions. The spectroscopic experiment for measuring the longitudinal cross-correlation rate constant for 1H-15N dipolar/15N chemical shift anisotropy interference is based on the approach for measuring the transverse cross-correlation rate constant (Tjandra, N.; Szabo, A.; Bax, A. J. Am. Chem. Soc. 1996, 118, 6986-6991) but incorporates a novel method for averaging the relaxation rates of longitudinal magnetization and two spin order. Application of this technique to Escherichia coli ribonuclease H affords an improved description of rotational diffusion anisotropy and permits a more accurate assessment of chemical exchange in this molecule. The results definitively demonstrate that amino acid residues K60 and W90 are subject to conformational exchange processes, whereas increased transverse relaxation rates for residues in the helix α(D) arise from anisotropic rotational diffusion.

Original languageEnglish (US)
Pages (from-to)7905-7915
Number of pages11
JournalJournal of the American Chemical Society
Volume120
Issue number31
DOIs
StatePublished - Aug 12 1998
Externally publishedYes

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Anisotropy
Chemical shift
Macromolecules
Tensors
Ion exchange
Rate constants
Biomolecular Nuclear Magnetic Resonance
Ribonuclease H
Escherichia coli
Nuclear magnetic resonance spectroscopy
Protons
Amino acids
Magnetization
Magnetic Resonance Spectroscopy
Amino Acids
Molecules
Experiments

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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title = "Longitudinal and transverse 1H-15N dipolar/15N chemical shift anisotropy relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules",
abstract = "High-resolution proton-detected heteronuclear correlation NMR spectroscopy allows the measurement of 15N spin relaxation rates at multiple sites throughout a biological macromolecule. The rate constants are determined by stochastic internal motions on time scales of picoseconds to nanoseconds, overall molecular rotational diffusion on time scales of nanoseconds, and chemical exchange rates on time scales of microseconds to milliseconds. A new method has been developed for distinguishing the contributions of chemical exchange from the contributions due to anisotropic rotational diffusion by measuring both longitudinal and transverse interference between the 1H-15N dipolar and 15N chemical shift anisotropy interactions. The spectroscopic experiment for measuring the longitudinal cross-correlation rate constant for 1H-15N dipolar/15N chemical shift anisotropy interference is based on the approach for measuring the transverse cross-correlation rate constant (Tjandra, N.; Szabo, A.; Bax, A. J. Am. Chem. Soc. 1996, 118, 6986-6991) but incorporates a novel method for averaging the relaxation rates of longitudinal magnetization and two spin order. Application of this technique to Escherichia coli ribonuclease H affords an improved description of rotational diffusion anisotropy and permits a more accurate assessment of chemical exchange in this molecule. The results definitively demonstrate that amino acid residues K60 and W90 are subject to conformational exchange processes, whereas increased transverse relaxation rates for residues in the helix α(D) arise from anisotropic rotational diffusion.",
author = "Kroenke, {Christopher (Chris)} and Loria, {J. Patrick} and Lee, {Larry K.} and Mark Rance and Palmer, {Arthur G.}",
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T1 - Longitudinal and transverse 1H-15N dipolar/15N chemical shift anisotropy relaxation interference

T2 - Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules

AU - Kroenke, Christopher (Chris)

AU - Loria, J. Patrick

AU - Lee, Larry K.

AU - Rance, Mark

AU - Palmer, Arthur G.

PY - 1998/8/12

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AB - High-resolution proton-detected heteronuclear correlation NMR spectroscopy allows the measurement of 15N spin relaxation rates at multiple sites throughout a biological macromolecule. The rate constants are determined by stochastic internal motions on time scales of picoseconds to nanoseconds, overall molecular rotational diffusion on time scales of nanoseconds, and chemical exchange rates on time scales of microseconds to milliseconds. A new method has been developed for distinguishing the contributions of chemical exchange from the contributions due to anisotropic rotational diffusion by measuring both longitudinal and transverse interference between the 1H-15N dipolar and 15N chemical shift anisotropy interactions. The spectroscopic experiment for measuring the longitudinal cross-correlation rate constant for 1H-15N dipolar/15N chemical shift anisotropy interference is based on the approach for measuring the transverse cross-correlation rate constant (Tjandra, N.; Szabo, A.; Bax, A. J. Am. Chem. Soc. 1996, 118, 6986-6991) but incorporates a novel method for averaging the relaxation rates of longitudinal magnetization and two spin order. Application of this technique to Escherichia coli ribonuclease H affords an improved description of rotational diffusion anisotropy and permits a more accurate assessment of chemical exchange in this molecule. The results definitively demonstrate that amino acid residues K60 and W90 are subject to conformational exchange processes, whereas increased transverse relaxation rates for residues in the helix α(D) arise from anisotropic rotational diffusion.

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