Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 342126
Title Exploring the local conformational space of a membrane protein by site-directed spin labeling
Author(s) Stopar, D.; Strancar, J.; Spruijt, R.B.; Hemminga, M.A.
Source Journal of Chemical Information and Modeling 45 (2005)5. - ISSN 1549-9596 - p. 1621 - 1627.
Department(s) Biophysics
Publication type Refereed Article in a scientific journal
Publication year 2005
Keyword(s) major coat protein - lipid bilayers - cytoplasmic membrane - escherichia-coli - m13 - dynamics - bacteriophage-m13 - spectroscopy - epr - micelles
Abstract Molecular modeling based on a hybrid evolutionary optimization and an information condensation algorithm, called GHOST, of spin label ESR spectra was applied to study the structure and dynamics of membrane proteins. The new method is capable of providing detailed molecular information about the conformational space of the spin-labeled segment of the protein in a membrane system. The method is applied to spin-labeled bacteriophage M13 major coat protein, which is used as a model membrane protein. Single cysteine mutants of the coat protein were labeled with nitroxide spin labels and incorporated in 1,2-dioleoyl-sn- glycero-3-phosphocholine (DOPC) bilayers. The new computational method allows us to monitor distributions of local spatial constraints and molecular mobility, in addition to information about the location of the protein in a membrane. Furthermore, the results suggest that different local conformations may coexist in the membrane protein. The knowledge of different local conformations may help us to better understand the function - structure relationship of membrane proteins.
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