Novel relaxation compensated method to measure proton exchange rates in biomolecules based on decorrelation of heteronuclear two-spin order

Viswanathan V Krishnan, Monique Cosman

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A combined experiment based on decorrelation of heteronuclear two-spin order and a new analysis method is presented for measuring accurate rapid amide proton exchange rates (kHH ex = kex) in 15N-labeled biomolecules, such as proteins or nucleic acids, in water. The term 'decorrelation' is defined as the loss of the initial correlation between a labile biomolecule proton and its coupled nitrogen when they are separated by intermolecular chemical exchange with water. The NMR pulse sequence [DECORrelated EXchange SpectroscopY (DECOREXSY)] measures the decay of the heteronuclear two-spin order terms with minimal interference effects from relaxation processes and solvent-induced artifacts. The new analysis protocol based on backbone relaxation measurements is introduced to compensate for relaxation contributions to the exchange rates that are otherwise inseparable. This simple and straightforward scheme has several potential applications in protein folding and biomolecular recognition and binding studies, and fills the need for a sensitive experiment to measure absolute fast-amide proton exchange rates predominantly on the sub-millisecond time-scale.

Original languageEnglish (US)
Pages (from-to)789-794
Number of pages6
JournalMagnetic Resonance in Chemistry
Volume38
Issue number9
StatePublished - Sep 2000
Externally publishedYes

Fingerprint

Biomolecules
Protons
Ion exchange
Amides
amides
protons
proteins
Protein folding
Water
Nucleic acids
nucleic acids
Relaxation processes
folding
Nucleic Acids
water
artifacts
Nitrogen
Experiments
Nuclear magnetic resonance
Spectroscopy

Keywords

  • N NMR
  • H NMR
  • Biomolecule
  • Decorrelation
  • NMR
  • Two-spin order
  • Water exchange

ASJC Scopus subject areas

  • Chemistry(all)
  • Physical and Theoretical Chemistry
  • Spectroscopy

Cite this

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title = "Novel relaxation compensated method to measure proton exchange rates in biomolecules based on decorrelation of heteronuclear two-spin order",
abstract = "A combined experiment based on decorrelation of heteronuclear two-spin order and a new analysis method is presented for measuring accurate rapid amide proton exchange rates (kHH ex = kex) in 15N-labeled biomolecules, such as proteins or nucleic acids, in water. The term 'decorrelation' is defined as the loss of the initial correlation between a labile biomolecule proton and its coupled nitrogen when they are separated by intermolecular chemical exchange with water. The NMR pulse sequence [DECORrelated EXchange SpectroscopY (DECOREXSY)] measures the decay of the heteronuclear two-spin order terms with minimal interference effects from relaxation processes and solvent-induced artifacts. The new analysis protocol based on backbone relaxation measurements is introduced to compensate for relaxation contributions to the exchange rates that are otherwise inseparable. This simple and straightforward scheme has several potential applications in protein folding and biomolecular recognition and binding studies, and fills the need for a sensitive experiment to measure absolute fast-amide proton exchange rates predominantly on the sub-millisecond time-scale.",
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N2 - A combined experiment based on decorrelation of heteronuclear two-spin order and a new analysis method is presented for measuring accurate rapid amide proton exchange rates (kHH ex = kex) in 15N-labeled biomolecules, such as proteins or nucleic acids, in water. The term 'decorrelation' is defined as the loss of the initial correlation between a labile biomolecule proton and its coupled nitrogen when they are separated by intermolecular chemical exchange with water. The NMR pulse sequence [DECORrelated EXchange SpectroscopY (DECOREXSY)] measures the decay of the heteronuclear two-spin order terms with minimal interference effects from relaxation processes and solvent-induced artifacts. The new analysis protocol based on backbone relaxation measurements is introduced to compensate for relaxation contributions to the exchange rates that are otherwise inseparable. This simple and straightforward scheme has several potential applications in protein folding and biomolecular recognition and binding studies, and fills the need for a sensitive experiment to measure absolute fast-amide proton exchange rates predominantly on the sub-millisecond time-scale.

AB - A combined experiment based on decorrelation of heteronuclear two-spin order and a new analysis method is presented for measuring accurate rapid amide proton exchange rates (kHH ex = kex) in 15N-labeled biomolecules, such as proteins or nucleic acids, in water. The term 'decorrelation' is defined as the loss of the initial correlation between a labile biomolecule proton and its coupled nitrogen when they are separated by intermolecular chemical exchange with water. The NMR pulse sequence [DECORrelated EXchange SpectroscopY (DECOREXSY)] measures the decay of the heteronuclear two-spin order terms with minimal interference effects from relaxation processes and solvent-induced artifacts. The new analysis protocol based on backbone relaxation measurements is introduced to compensate for relaxation contributions to the exchange rates that are otherwise inseparable. This simple and straightforward scheme has several potential applications in protein folding and biomolecular recognition and binding studies, and fills the need for a sensitive experiment to measure absolute fast-amide proton exchange rates predominantly on the sub-millisecond time-scale.

KW - N NMR

KW - H NMR

KW - Biomolecule

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KW - NMR

KW - Two-spin order

KW - Water exchange

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