ArticleEuropean biophysics journal : EBJ2009
Protein dynamics of a beta-sheet protein.
Article in European biophysics journal : EBJ, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Distinct Local and Global Dynamics of α-Helices and β-Sheets in Poly(γ-benzyl-l-glutamate) Peptides.Biomacromolecules · 2026Article
- Conformational variation of proteins at room temperature is not dominated by radiation damage.Journal of synchrotron radiation · 2017Article
- Ensemble MD simulations restrained via crystallographic data: accurate structure leads to accurate dynamics.Protein science : a publication of the Protein Society · 2014Article
- Enzyme transient state kinetics in crystal and solution from the perspective of a time-resolved crystallographer.Structural dynamics (Melville, N.Y.) · 2014Article
- Nuclear inelastic scattering and Mössbauer spectroscopy as local probes for ligand binding modes and electronic properties in proteins: vibrational behavior of a ferriheme center inside a β-barrel protein.Journal of the American Chemical Society · 2012Article
- Temperature-dependent macromolecular X-ray crystallography.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Five-dimensional crystallography.Acta crystallographica. Section A, Foundations of crystallography · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rhodnius prolixus Nitrophorin 4 (abbreviated NP4) is an almost pure beta-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 beta-sheet protein with the pure alpha-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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Registered trials
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