Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy. / Bugge, Katrine Østergaard; Steinocher, Helena; Brooks, Andrew J.; Lindorff-Larsen, Kresten; Kragelund, Birthe Brandt.

In: Analytical Chemistry, Vol. 87, No. 18, 2015, p. 9126–9131.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Bugge, KØ, Steinocher, H, Brooks, AJ, Lindorff-Larsen, K & Kragelund, BB 2015, 'Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy', Analytical Chemistry, vol. 87, no. 18, pp. 9126–9131. https://doi.org/10.1021/acs.analchem.5b02365

APA

Bugge, K. Ø., Steinocher, H., Brooks, A. J., Lindorff-Larsen, K., & Kragelund, B. B. (2015). Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy. Analytical Chemistry, 87(18), 9126–9131. https://doi.org/10.1021/acs.analchem.5b02365

Vancouver

Bugge KØ, Steinocher H, Brooks AJ, Lindorff-Larsen K, Kragelund BB. Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy. Analytical Chemistry. 2015;87(18):9126–9131. https://doi.org/10.1021/acs.analchem.5b02365

Author

Bugge, Katrine Østergaard ; Steinocher, Helena ; Brooks, Andrew J. ; Lindorff-Larsen, Kresten ; Kragelund, Birthe Brandt. / Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy. In: Analytical Chemistry. 2015 ; Vol. 87, No. 18. pp. 9126–9131.

Bibtex

@article{a146422eb89f4933b7f4e5a67247faf1,
title = "Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy",
abstract = "Despite the biological and pharmaceutical significance of membrane proteins, their tertiary structures constitute less than 3% of known structures. One of the major obstacles for initiating structural studies of membrane proteins by NMR spectroscopy is the generation of high amounts of isotope-labeled protein. In this work, we have exploited the hydrophobic nature of membrane proteins to develop a simple and efficient production scheme for isotope-labeled single-pass transmembrane domains (TMDs) with or without intrinsically disordered regions. We have evaluated the applicability and limitations of the strategy using seven membrane protein variants that differ in their overall hydrophobicity and length and show a recovery for suitable variants of >70%. The developed production scheme is cost-efficient and easy to implement and has the potential to facilitate an increase in the number of structures of single-pass TMDs, which are difficult to solve by other means.",
author = "Bugge, {Katrine {\O}stergaard} and Helena Steinocher and Brooks, {Andrew J.} and Kresten Lindorff-Larsen and Kragelund, {Birthe Brandt}",
year = "2015",
doi = "10.1021/acs.analchem.5b02365",
language = "English",
volume = "87",
pages = "9126–9131",
journal = "Industrial And Engineering Chemistry Analytical Edition",
issn = "0003-2700",
publisher = "American Chemical Society",
number = "18",

}

RIS

TY - JOUR

T1 - Exploiting hydrophobicity for efficient production of transmembrane helices for structure determination by NMR spectroscopy

AU - Bugge, Katrine Østergaard

AU - Steinocher, Helena

AU - Brooks, Andrew J.

AU - Lindorff-Larsen, Kresten

AU - Kragelund, Birthe Brandt

PY - 2015

Y1 - 2015

N2 - Despite the biological and pharmaceutical significance of membrane proteins, their tertiary structures constitute less than 3% of known structures. One of the major obstacles for initiating structural studies of membrane proteins by NMR spectroscopy is the generation of high amounts of isotope-labeled protein. In this work, we have exploited the hydrophobic nature of membrane proteins to develop a simple and efficient production scheme for isotope-labeled single-pass transmembrane domains (TMDs) with or without intrinsically disordered regions. We have evaluated the applicability and limitations of the strategy using seven membrane protein variants that differ in their overall hydrophobicity and length and show a recovery for suitable variants of >70%. The developed production scheme is cost-efficient and easy to implement and has the potential to facilitate an increase in the number of structures of single-pass TMDs, which are difficult to solve by other means.

AB - Despite the biological and pharmaceutical significance of membrane proteins, their tertiary structures constitute less than 3% of known structures. One of the major obstacles for initiating structural studies of membrane proteins by NMR spectroscopy is the generation of high amounts of isotope-labeled protein. In this work, we have exploited the hydrophobic nature of membrane proteins to develop a simple and efficient production scheme for isotope-labeled single-pass transmembrane domains (TMDs) with or without intrinsically disordered regions. We have evaluated the applicability and limitations of the strategy using seven membrane protein variants that differ in their overall hydrophobicity and length and show a recovery for suitable variants of >70%. The developed production scheme is cost-efficient and easy to implement and has the potential to facilitate an increase in the number of structures of single-pass TMDs, which are difficult to solve by other means.

U2 - 10.1021/acs.analchem.5b02365

DO - 10.1021/acs.analchem.5b02365

M3 - Journal article

C2 - 26309151

VL - 87

SP - 9126

EP - 9131

JO - Industrial And Engineering Chemistry Analytical Edition

JF - Industrial And Engineering Chemistry Analytical Edition

SN - 0003-2700

IS - 18

ER -

ID: 143918901