Proteins in a brave new surfactant world

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Proteins in a brave new surfactant world. / Otzen, Daniel E.

In: Current Opinion in Colloid & Interface Science, Vol. 20, No. 3, 01.06.2015, p. 161-169.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Otzen, DE 2015, 'Proteins in a brave new surfactant world', Current Opinion in Colloid & Interface Science, vol. 20, no. 3, pp. 161-169. https://doi.org/10.1016/j.cocis.2015.07.003

APA

Otzen, D. E. (2015). Proteins in a brave new surfactant world. Current Opinion in Colloid & Interface Science, 20(3), 161-169. https://doi.org/10.1016/j.cocis.2015.07.003

CBE

Otzen DE. 2015. Proteins in a brave new surfactant world. Current Opinion in Colloid & Interface Science. 20(3):161-169. https://doi.org/10.1016/j.cocis.2015.07.003

MLA

Otzen, Daniel E. "Proteins in a brave new surfactant world". Current Opinion in Colloid & Interface Science. 2015, 20(3). 161-169. https://doi.org/10.1016/j.cocis.2015.07.003

Vancouver

Otzen DE. Proteins in a brave new surfactant world. Current Opinion in Colloid & Interface Science. 2015 Jun 1;20(3):161-169. https://doi.org/10.1016/j.cocis.2015.07.003

Author

Otzen, Daniel E. / Proteins in a brave new surfactant world. In: Current Opinion in Colloid & Interface Science. 2015 ; Vol. 20, No. 3. pp. 161-169.

Bibtex

@article{312a2dc15f134fc6a5dce37846c28f38,
title = "Proteins in a brave new surfactant world",
abstract = "This review discusses emerging topics within the field of protein-surfactant interactions over the last 4-5. years. The application of small-angle x-ray scattering has allowed us to construct ever more detailed models of the structures of different protein-surfactant complexes and has revealed common features shared between electrophoretic protein-SDS complexes and liprotides (complexes between lipids and partially denatured proteins), namely a generic core-shell structure which can also form beads on a string. SDS emerges as the best surfactant for gel electrophoresis from a series of studies comparing it with surfactants differing in chain length, degree of branching, and fluorination, as well as dodecyl sulfate with different counterions. Nevertheless, these surfactants possess useful properties for alternative applications. SDS also continues to serve as a useful tool for systematic folding/unfolding studies of membrane proteins together with the non-ionic surfactant dodecyl maltoside, as well as for studying hyperstable kinetically trapped proteins. Biosurfactants are coming to the fore as sustainable alternatives to chemical surfactants and show unique properties toward proteins that combine aspects of both ionic and non-ionic surfactants.",
keywords = "Biosurfactants, Branched surfactants, Membrane proteins, Mixed micelles, SDS binding, Small-angle scattering",
author = "Otzen, {Daniel E.}",
year = "2015",
month = "6",
day = "1",
doi = "10.1016/j.cocis.2015.07.003",
language = "English",
volume = "20",
pages = "161--169",
journal = "Current Opinion in Colloid & Interface Science",
issn = "1359-0294",
publisher = "Pergamon Press",
number = "3",

}

RIS

TY - JOUR

T1 - Proteins in a brave new surfactant world

AU - Otzen, Daniel E.

PY - 2015/6/1

Y1 - 2015/6/1

N2 - This review discusses emerging topics within the field of protein-surfactant interactions over the last 4-5. years. The application of small-angle x-ray scattering has allowed us to construct ever more detailed models of the structures of different protein-surfactant complexes and has revealed common features shared between electrophoretic protein-SDS complexes and liprotides (complexes between lipids and partially denatured proteins), namely a generic core-shell structure which can also form beads on a string. SDS emerges as the best surfactant for gel electrophoresis from a series of studies comparing it with surfactants differing in chain length, degree of branching, and fluorination, as well as dodecyl sulfate with different counterions. Nevertheless, these surfactants possess useful properties for alternative applications. SDS also continues to serve as a useful tool for systematic folding/unfolding studies of membrane proteins together with the non-ionic surfactant dodecyl maltoside, as well as for studying hyperstable kinetically trapped proteins. Biosurfactants are coming to the fore as sustainable alternatives to chemical surfactants and show unique properties toward proteins that combine aspects of both ionic and non-ionic surfactants.

AB - This review discusses emerging topics within the field of protein-surfactant interactions over the last 4-5. years. The application of small-angle x-ray scattering has allowed us to construct ever more detailed models of the structures of different protein-surfactant complexes and has revealed common features shared between electrophoretic protein-SDS complexes and liprotides (complexes between lipids and partially denatured proteins), namely a generic core-shell structure which can also form beads on a string. SDS emerges as the best surfactant for gel electrophoresis from a series of studies comparing it with surfactants differing in chain length, degree of branching, and fluorination, as well as dodecyl sulfate with different counterions. Nevertheless, these surfactants possess useful properties for alternative applications. SDS also continues to serve as a useful tool for systematic folding/unfolding studies of membrane proteins together with the non-ionic surfactant dodecyl maltoside, as well as for studying hyperstable kinetically trapped proteins. Biosurfactants are coming to the fore as sustainable alternatives to chemical surfactants and show unique properties toward proteins that combine aspects of both ionic and non-ionic surfactants.

KW - Biosurfactants

KW - Branched surfactants

KW - Membrane proteins

KW - Mixed micelles

KW - SDS binding

KW - Small-angle scattering

UR - http://www.scopus.com/inward/record.url?scp=84941880766&partnerID=8YFLogxK

U2 - 10.1016/j.cocis.2015.07.003

DO - 10.1016/j.cocis.2015.07.003

M3 - Journal article

AN - SCOPUS:84941880766

VL - 20

SP - 161

EP - 169

JO - Current Opinion in Colloid & Interface Science

JF - Current Opinion in Colloid & Interface Science

SN - 1359-0294

IS - 3

ER -