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Protein dynamics of a β-sheet protein

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Abstract

Rhodnius prolixus Nitrophorin 4 (abbreviated NP4) is an almost pure β-sheet heme protein. Its dynamics is investigated by X-ray structure determination at eight different temperatures from 122 to 304 K and by means of Mössbauer spectroscopy. A comparison of this β-sheet protein with the pure α-helical protein myoglobin (abbreviated Mbmet) is performed. The mean square displacement derived from the Mössbauer spectra increases linearly with temperature below a characteristic temperature T c. It is about 10 K larger than that of myoglobin. Above T c the mean square displacements increase dramatically. The Mössbauer spectra are analyzed by a two state model. The increased mean square displacements are caused by very slow motions occurring on a time scale faster than 140 ns. With respect to these motions NP4 shows the same protein specific modes as Mbmet. There is, however, a difference in the fast vibration regime. The B values found in the X-ray structures vary linearly over the entire temperature range. The mean square displacements in NP4 increase with slopes which are 60% larger than those observed for Mbmet. This indicates that nitrophorin has a larger structural distribution which makes it more flexible than myoglobin.

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Acknowledgment

This research was supported by the German Research Foundation (DFG) under Grants No. PA 178/28-1 and PA 178/28-2.

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Authors and Affiliations

  1. Physics Department E17, Technical University Munich, 85747, Garching, Germany

    Marius Schmidt, Klaus Achterhold, Valeriy Prusakov & Fritz G. Parak

  2. University of Wisconsin-Milwaukee, Milwaukee, WI, 53211, USA

    Marius Schmidt

  3. Institute of Chemical Physics, RAS, 117334, Moscow, Russia

    Valeriy Prusakov

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  1. Marius Schmidt
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  2. Klaus Achterhold
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Correspondence to Fritz G. Parak.

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Schmidt, M., Achterhold, K., Prusakov, V. et al. Protein dynamics of a β-sheet protein. Eur Biophys J 38, 687–700 (2009). https://doi.org/10.1007/s00249-009-0427-z

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