1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa

Gettins, Peter G.W.

doi:10.1016/0141-8130(94)90027-2

Cited by 6 publications

(2 citation statements)

References 70 publications

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“…Incorporation of fluorinated methionine analogues into the chemotactic fMet-Leu-Phe tripeptide enhance the ability of this peptide to attract neutrophils [5]. Additionally, fluorinated amino acids have been utilized extensively in 19 F NMR investigations into the structural and dynamic properties of proteins in solution [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Experimental and theoretical studies on inversion dynamics of dichloro(l-difluoromethionine-N,S)platinum(II) and dichloro(l-trifluoromethionine-N,S)platinum(II) complexes

Vaughan

Robertson

Honek

2007

Journal of Fluorine Chemistry

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Section: Introductionmentioning

confidence: 99%

Experimental and theoretical studies on inversion dynamics of dichloro(l-difluoromethionine-N,S)platinum(II) and dichloro(l-trifluoromethionine-N,S)platinum(II) complexes

Vaughan

Robertson

Honek

2007

Journal of Fluorine Chemistry

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“…Fluorine‐19 is a spin 1/2 nucleus that is nonnative to proteins, so that spectra give no background signals and are easy to assign. Due to its high gyromagnetic ratio, the sensitivity of 19 F is comparable to 1 H but with larger chemical shift dispersion, which makes it more sensitive to the chemical environment (9).…”

Section: Introductionmentioning

confidence: 99%

¹⁹F‐MAS NMR on Proteorhodopsin: Enhanced Protocol for Site‐Specific Labeling for General Application to Membrane Proteins^†

Hellmich¹,

Pfleger²,

Glaubitz³

2009

Photochem & Photobiology

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Proteorhodopsin (PR) is a light-driven proton pump found in near-surface marine gamma-proteobacteria. The green absorbing variant has three cysteines at positions 107, 156 and 175. We probed the accessibility of these residues by (19)F-MAS NMR. For this purpose, an efficient but simple protocol for chemical fluorine labeling of accessible cysteines in membrane proteins was established. This one-step reaction was applied to detergent-solubilized PR before reconstitution into phospholipids. All three cysteines could be labeled and showed distinct (19)F chemical shifts with different integral intensities. The accessibility of these cysteines is discussed in the context of a homology model. With the chemical cysteine labeling procedure shown here, an attractive option for site-directed solid-state NMR studies on other membrane proteins is offered due to the high intrinsic sensitivity of (19)F-MAS NMR.

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Insertion of an unnatural amino acid into the protein structure: preparation and properties of 3-fluorotyrosine-containing organophosphate hydrolase

2006

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1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa

Cited by 6 publications

References 70 publications

Experimental and theoretical studies on inversion dynamics of dichloro(l-difluoromethionine-N,S)platinum(II) and dichloro(l-trifluoromethionine-N,S)platinum(II) complexes

Experimental and theoretical studies on inversion dynamics of dichloro(l-difluoromethionine-N,S)platinum(II) and dichloro(l-trifluoromethionine-N,S)platinum(II) complexes

¹⁹F‐MAS NMR on Proteorhodopsin: Enhanced Protocol for Site‐Specific Labeling for General Application to Membrane Proteins^†

Insertion of an unnatural amino acid into the protein structure: preparation and properties of 3-fluorotyrosine-containing organophosphate hydrolase

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1H- and 19F-NMR approaches to the study of the structure of proteins larger than 25 kDa

Cited by 6 publications

References 70 publications

Experimental and theoretical studies on inversion dynamics of dichloro(l-difluoromethionine-N,S)platinum(II) and dichloro(l-trifluoromethionine-N,S)platinum(II) complexes

Experimental and theoretical studies on inversion dynamics of dichloro(l-difluoromethionine-N,S)platinum(II) and dichloro(l-trifluoromethionine-N,S)platinum(II) complexes

19F‐MAS NMR on Proteorhodopsin: Enhanced Protocol for Site‐Specific Labeling for General Application to Membrane Proteins†

Insertion of an unnatural amino acid into the protein structure: preparation and properties of 3-fluorotyrosine-containing organophosphate hydrolase

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Product

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¹⁹F‐MAS NMR on Proteorhodopsin: Enhanced Protocol for Site‐Specific Labeling for General Application to Membrane Proteins^†