The influence of poly(ethylene glycol) on the micelle formation of alkyl maltosides used in membrane protein crystallization
| dc.contributor.author | Müh, Frank | |
| dc.contributor.author | DiFiore, Dörte | |
| dc.contributor.author | Zouni, Athina | |
| dc.date.accessioned | 2017-10-25T06:27:45Z | |
| dc.date.available | 2017-10-25T06:27:45Z | |
| dc.date.issued | 2015 | |
| dc.description | Dieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG geförderten) Allianz- bzw. Nationallizenz frei zugänglich. | de |
| dc.description | This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively. | en |
| dc.description.abstract | With the aim of better understanding the phase behavior of alkyl maltosides (n-alkyl-beta-D-maltosides, C(n)G(2)) under the conditions of membrane protein crystallization, we studied the influence of poly(ethylene glycol) (PEG) 2000, a commonly used precipitating agent, on the critical micelle concentration (CMC) of the alkyl maltosides by systematic variation of the number n of carbon atoms in the alkyl chain (n = 10, 11, and 12) and the concentration of PEG2000 (chi) in a buffer suitable for the crystallization of cyanobacterial photosystem II. CMC measurements were based on established fluorescence techniques using pyrene and 8-anilinonaphthalene-1-sulfonate (ANS). We found an increase of the CMC with increasing PEG concentration according to ln(CMC/CMC0) = k(P)chi, where CMC0 is the CMC in the absence of PEG and k(P) is a constant that we termed the "polymer constant". In parallel, we measured the influence of PEG2000 on the surface tension of detergent-free buffer solutions. At PEG concentrations chi > 1% w/v, the surface pressure pi(s)(chi) = gamma(0) - gamma(chi) was found to depend linearly on the PEG concentration according to pi(s)(chi) = kappa chi + pi(s)(0), where gamma(0) is the surface tension in the absence of PEG. Based on a molecular thermodynamic modeling, CMC shifts and surface pressure due to PEG are related, and it is shown that k(P) = kappa c(n) + eta, where c(n) is a detergent-specific constant depending inter alia on the alkyl chain length n and eta is a correction for molarity. Thus, knowledge of the surface pressure in the absence of a detergent allows for the prediction of the CMC shift. The PEG effect on the CMC is discussed concerning its molecular origin and its implications for membrane protein solubilization and crystallization. | en |
| dc.description.sponsorship | DFG, SFB 429, Molekulare Physiologie, Energetik und Regulation primärer pflanzlicher Stoffwechselprozesse | en |
| dc.description.sponsorship | DFG, SFB 498, Protein-Kofaktor-Wechselwirkungen in biologischen Prozessen | en |
| dc.description.sponsorship | DFG, SFB 1078, Proteinfunktion durch Protonierungsdynamik | en |
| dc.description.sponsorship | DFG, EXC 314, Unifying Concepts in Catalysis | en |
| dc.description.sponsorship | BMBF, 031A154B, Basistechnologien Forschertandem: Nutzung von Sonnenenergie für die Bioelektrokatalyse - Entwicklung von Photo-Bioelektrodenstrukturen für die Synthese | en |
| dc.identifier.eissn | 1463-9084 | |
| dc.identifier.issn | 1463-9076 | |
| dc.identifier.pmid | 25865704 | |
| dc.identifier.uri | https://depositonce.tu-berlin.de/handle/11303/6965 | |
| dc.identifier.uri | http://dx.doi.org/10.14279/depositonce-6304 | |
| dc.language.iso | en | |
| dc.rights.uri | http://rightsstatements.org/vocab/InC/1.0/ | |
| dc.subject.ddc | 540 Chemie und zugeordnete Wissenschaften | de |
| dc.title | The influence of poly(ethylene glycol) on the micelle formation of alkyl maltosides used in membrane protein crystallization | en |
| dc.type | Article | en |
| dc.type.version | publishedVersion | en |
| dcterms.bibliographicCitation.doi | 10.1039/c5cp00431d | |
| dcterms.bibliographicCitation.issue | 17 | |
| dcterms.bibliographicCitation.journaltitle | Physical chemistry, chemical physics | en |
| dcterms.bibliographicCitation.originalpublishername | Royal Society of Chemistry | de |
| dcterms.bibliographicCitation.originalpublisherplace | Cambridge | de |
| dcterms.bibliographicCitation.pageend | 11691 | |
| dcterms.bibliographicCitation.pagestart | 11678 | |
| dcterms.bibliographicCitation.volume | 17 | |
| tub.accessrights.dnb | domain | |
| tub.affiliation | Fak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Physikalische Chemie / Biophysikalische Chemie | de |
| tub.affiliation.faculty | Fak. 2 Mathematik und Naturwissenschaften | de |
| tub.affiliation.group | FG Physikalische Chemie / Biophysikalische Chemie | de |
| tub.affiliation.institute | Inst. Chemie | de |
| tub.publisher.universityorinstitution | Technische Universität Berlin |
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