Cation Binding Induced Changes in 15 N CSA in a Membrane-Bound Polypeptide

Fang Tian, T. A. Cross

Research output: Contribution to journalEditorial

13 Citations (Scopus)

Abstract

Cation binding to the monovalent cation selective channel, gramicidin A, is shown to induce changes in the dipolar and chemical shift observables from uniformly aligned samples. While these changes could be the result of structural or dynamic changes, they are shown to be primarily induced by through-bond polarizability effects when cations are solvated by the carbonyl oxygens of the peptide backbone. Upon cation binding partial charges are changed throughout the peptide plane, inducing large changes in the 13 C 1 chemical shifts, smaller changes in the 15 N chemical shifts, and even smaller effects for the 15 N- 13 C 1 and 15 N- 2 H dipolar interactions. These conclusions are substantiated by characterizing the 15 N chemical shift tensors in the presence and absence of cations in fast-frozen lipid bilayer preparations of gramicidin A.

Original languageEnglish (US)
Pages (from-to)535-540
Number of pages6
JournalJournal of Magnetic Resonance
Volume135
Issue number2
DOIs
StatePublished - Jan 1 1998

Fingerprint

polypeptides
Chemical shift
Cations
chemical equilibrium
membranes
Membranes
Gramicidin
cations
Peptides
peptides
Monovalent Cations
Lipid bilayers
Lipid Bilayers
Tensors
lipids
Oxygen
tensors
preparation
shift
oxygen

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics

Cite this

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title = "Cation Binding Induced Changes in 15 N CSA in a Membrane-Bound Polypeptide",
abstract = "Cation binding to the monovalent cation selective channel, gramicidin A, is shown to induce changes in the dipolar and chemical shift observables from uniformly aligned samples. While these changes could be the result of structural or dynamic changes, they are shown to be primarily induced by through-bond polarizability effects when cations are solvated by the carbonyl oxygens of the peptide backbone. Upon cation binding partial charges are changed throughout the peptide plane, inducing large changes in the 13 C 1 chemical shifts, smaller changes in the 15 N chemical shifts, and even smaller effects for the 15 N- 13 C 1 and 15 N- 2 H dipolar interactions. These conclusions are substantiated by characterizing the 15 N chemical shift tensors in the presence and absence of cations in fast-frozen lipid bilayer preparations of gramicidin A.",
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Cation Binding Induced Changes in 15 N CSA in a Membrane-Bound Polypeptide . / Tian, Fang; Cross, T. A.

In: Journal of Magnetic Resonance, Vol. 135, No. 2, 01.01.1998, p. 535-540.

Research output: Contribution to journalEditorial

TY - JOUR

T1 - Cation Binding Induced Changes in 15 N CSA in a Membrane-Bound Polypeptide

AU - Tian, Fang

AU - Cross, T. A.

PY - 1998/1/1

Y1 - 1998/1/1

N2 - Cation binding to the monovalent cation selective channel, gramicidin A, is shown to induce changes in the dipolar and chemical shift observables from uniformly aligned samples. While these changes could be the result of structural or dynamic changes, they are shown to be primarily induced by through-bond polarizability effects when cations are solvated by the carbonyl oxygens of the peptide backbone. Upon cation binding partial charges are changed throughout the peptide plane, inducing large changes in the 13 C 1 chemical shifts, smaller changes in the 15 N chemical shifts, and even smaller effects for the 15 N- 13 C 1 and 15 N- 2 H dipolar interactions. These conclusions are substantiated by characterizing the 15 N chemical shift tensors in the presence and absence of cations in fast-frozen lipid bilayer preparations of gramicidin A.

AB - Cation binding to the monovalent cation selective channel, gramicidin A, is shown to induce changes in the dipolar and chemical shift observables from uniformly aligned samples. While these changes could be the result of structural or dynamic changes, they are shown to be primarily induced by through-bond polarizability effects when cations are solvated by the carbonyl oxygens of the peptide backbone. Upon cation binding partial charges are changed throughout the peptide plane, inducing large changes in the 13 C 1 chemical shifts, smaller changes in the 15 N chemical shifts, and even smaller effects for the 15 N- 13 C 1 and 15 N- 2 H dipolar interactions. These conclusions are substantiated by characterizing the 15 N chemical shift tensors in the presence and absence of cations in fast-frozen lipid bilayer preparations of gramicidin A.

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