Sampling the conformational space of membrane protein surfaces with the AFM.
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| Title: | Sampling the conformational space of membrane protein surfaces with the AFM. |
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| Authors: | Scheuring, Simon, Müller, Daniel J., Stahlberg, Henning, Engel, Hans-Andreas, Engel, Andreas |
| Source: | European Biophysics Journal. 2002, Vol. 31 Issue 3, p172. 7p. |
| Subjects: | Membrane proteins, Atomic force microscopy |
| Abstract: | The atomic force microscope acquires topographs of single native membrane proteins at subnanometer resolution. Owing to the high signal-to-noise ratio, such images allow the conformational space of membrane protein surfaces to be sampled. This is demonstrated by topographs of porin OmpF, aquaporin-Z, and bacteriorhodopsin, all recorded at a lateral resolution of <7 Å and a vertical resolution of ~1 Å. The amplitudes of the domain movements were estimated from a large number of single molecule topographs and the corresponding energy landscapes calculated. To visualize the motion of protein domains, movies were generated by similarity ranking of the observed protein configurations. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00249-001-0197-8. [ABSTRACT FROM AUTHOR] |
| Copyright of European Biophysics Journal is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Links: – Type: pdflink Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 6700186 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Sampling the conformational space of membrane protein surfaces with the AFM. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Scheuring%2C+Simon%22">Scheuring, Simon</searchLink><br /><searchLink fieldCode="AR" term="%22Müller%2C+Daniel+J%2E%22">Müller, Daniel J.</searchLink><br /><searchLink fieldCode="AR" term="%22Stahlberg%2C+Henning%22">Stahlberg, Henning</searchLink><br /><searchLink fieldCode="AR" term="%22Engel%2C+Hans-Andreas%22">Engel, Hans-Andreas</searchLink><br /><searchLink fieldCode="AR" term="%22Engel%2C+Andreas%22">Engel, Andreas</searchLink> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22European+Biophysics+Journal%22">European Biophysics Journal</searchLink>. 2002, Vol. 31 Issue 3, p172. 7p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Membrane+proteins%22">Membrane proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Atomic+force+microscopy%22">Atomic force microscopy</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: The atomic force microscope acquires topographs of single native membrane proteins at subnanometer resolution. Owing to the high signal-to-noise ratio, such images allow the conformational space of membrane protein surfaces to be sampled. This is demonstrated by topographs of porin OmpF, aquaporin-Z, and bacteriorhodopsin, all recorded at a lateral resolution of <7 Å and a vertical resolution of ~1 Å. The amplitudes of the domain movements were estimated from a large number of single molecule topographs and the corresponding energy landscapes calculated. To visualize the motion of protein domains, movies were generated by similarity ranking of the observed protein configurations. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00249-001-0197-8. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of European Biophysics Journal is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
| PLink | https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=6700186 |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1007/s00249-001-0197-8 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 7 StartPage: 172 Subjects: – SubjectFull: Membrane proteins Type: general – SubjectFull: Atomic force microscopy Type: general Titles: – TitleFull: Sampling the conformational space of membrane protein surfaces with the AFM. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Scheuring, Simon – PersonEntity: Name: NameFull: Müller, Daniel J. – PersonEntity: Name: NameFull: Stahlberg, Henning – PersonEntity: Name: NameFull: Engel, Hans-Andreas – PersonEntity: Name: NameFull: Engel, Andreas IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 06 Text: 2002 Type: published Y: 2002 Identifiers: – Type: issn-print Value: 01757571 Numbering: – Type: volume Value: 31 – Type: issue Value: 3 Titles: – TitleFull: European Biophysics Journal Type: main |
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