Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements

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Standard

Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements. / Teilum, Kaare; Brath, Ulrika; Lundström, Patrik; Akke, Mikael.

I: Journal of the American Chemical Society, Bind 128, Nr. 8, 2006, s. 2506-7.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Teilum, K, Brath, U, Lundström, P & Akke, M 2006, 'Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements', Journal of the American Chemical Society, bind 128, nr. 8, s. 2506-7. https://doi.org/10.1021/ja055660o

APA

Teilum, K., Brath, U., Lundström, P., & Akke, M. (2006). Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements. Journal of the American Chemical Society, 128(8), 2506-7. https://doi.org/10.1021/ja055660o

Vancouver

Teilum K, Brath U, Lundström P, Akke M. Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements. Journal of the American Chemical Society. 2006;128(8):2506-7. https://doi.org/10.1021/ja055660o

Author

Teilum, Kaare ; Brath, Ulrika ; Lundström, Patrik ; Akke, Mikael. / Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements. I: Journal of the American Chemical Society. 2006 ; Bind 128, Nr. 8. s. 2506-7.

Bibtex

@article{32fda0d0bd6611debda0000ea68e967b,
title = "Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements",
abstract = "Site-specific 13C labeling offers a desirable means of eliminating unwanted relaxation pathways and coherent magnetization transfer in NMR relaxation experiments. Here we use [1-13C]-glucose as the sole carbon source in the growth media for protein overexpression in Escherichia coli. The approach results in specific incorporation of 13C at isolated positions in the side chains of aromatic amino acids, which greatly simplifies the measurements and interpretation of 13C relaxation rates in these spin systems. The method is well suited for characterization of chemical exchange by CPMG or spin-lock relaxation methods. We validated the method by acquiring 13C rotating-frame relaxation dispersion data on the E140Q mutant of the C-terminal domain of calmodulin, which reveal conformational exchange dynamics with a time constant of 71 mus for Y138.",
author = "Kaare Teilum and Ulrika Brath and Patrik Lundstr{\"o}m and Mikael Akke",
note = "Keywords: Acyl Coenzyme A; Amino Acids, Aromatic; Animals; Calmodulin; Carbon Isotopes; Cattle; Escherichia coli; Glucose; Isotope Labeling; Nuclear Magnetic Resonance, Biomolecular; Phenylalanine; Protein Structure, Tertiary",
year = "2006",
doi = "10.1021/ja055660o",
language = "English",
volume = "128",
pages = "2506--7",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "8",

}

RIS

TY - JOUR

T1 - Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements

AU - Teilum, Kaare

AU - Brath, Ulrika

AU - Lundström, Patrik

AU - Akke, Mikael

N1 - Keywords: Acyl Coenzyme A; Amino Acids, Aromatic; Animals; Calmodulin; Carbon Isotopes; Cattle; Escherichia coli; Glucose; Isotope Labeling; Nuclear Magnetic Resonance, Biomolecular; Phenylalanine; Protein Structure, Tertiary

PY - 2006

Y1 - 2006

N2 - Site-specific 13C labeling offers a desirable means of eliminating unwanted relaxation pathways and coherent magnetization transfer in NMR relaxation experiments. Here we use [1-13C]-glucose as the sole carbon source in the growth media for protein overexpression in Escherichia coli. The approach results in specific incorporation of 13C at isolated positions in the side chains of aromatic amino acids, which greatly simplifies the measurements and interpretation of 13C relaxation rates in these spin systems. The method is well suited for characterization of chemical exchange by CPMG or spin-lock relaxation methods. We validated the method by acquiring 13C rotating-frame relaxation dispersion data on the E140Q mutant of the C-terminal domain of calmodulin, which reveal conformational exchange dynamics with a time constant of 71 mus for Y138.

AB - Site-specific 13C labeling offers a desirable means of eliminating unwanted relaxation pathways and coherent magnetization transfer in NMR relaxation experiments. Here we use [1-13C]-glucose as the sole carbon source in the growth media for protein overexpression in Escherichia coli. The approach results in specific incorporation of 13C at isolated positions in the side chains of aromatic amino acids, which greatly simplifies the measurements and interpretation of 13C relaxation rates in these spin systems. The method is well suited for characterization of chemical exchange by CPMG or spin-lock relaxation methods. We validated the method by acquiring 13C rotating-frame relaxation dispersion data on the E140Q mutant of the C-terminal domain of calmodulin, which reveal conformational exchange dynamics with a time constant of 71 mus for Y138.

U2 - 10.1021/ja055660o

DO - 10.1021/ja055660o

M3 - Journal article

C2 - 16492013

VL - 128

SP - 2506

EP - 2507

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 8

ER -

ID: 15288519