R
Reinhard Klement
Researcher at Max Planck Society
Publications - 21
Citations - 552
Reinhard Klement is an academic researcher from Max Planck Society. The author has contributed to research in topics: Base pair & Circular dichroism. The author has an hindex of 11, co-authored 21 publications receiving 508 citations.
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Journal ArticleDOI
Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged alpha-synuclein
M. J. Roberti,Carlos W. Bertoncini,Reinhard Klement,Elizabeth A. Jares-Erijman,Thomas M. Jovin +4 more
TL;DR: A recombinant α- synuclein bearing a tetracysteine target for fluorogenic biarsenical compounds offers the means for directly probing amyloid formation and interactions of α-synuclein with other proteins in living cells, the response to cellular stress and screening drugs for Parkinson disease.
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Actinomycin D binding to single-stranded DNA: sequence specificity and hemi-intercalation model from fluorescence and 1H NMR spectroscopy.
Randy M. Wadkins,Elizabeth A. Jares-Erijman,Reinhard Klement,Angelika Rüdiger,Thomas M. Jovin +4 more
TL;DR: A comparison of the measured chemical shifts with those estimated from ring-current calculations provided strong evidence for a hemi-intercalation of AMD between the A and G purine bases with a preference for one of two possible relative orientations.
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Dynamic Conformational Transitions of the EGF Receptor in Living Mammalian Cells Determined by FRET and Fluorescence Lifetime Imaging Microscopy
Iwona Ziomkiewicz,Anastasia Loman,Reinhard Klement,Cornelia Fritsch,Andrey S. Klymchenko,Gertrude Bunt,Thomas M. Jovin,Donna J. Arndt-Jovin +7 more
TL;DR: The data indicate that the unliganded domain I of the EGFR receptor is situated much closer to the membrane before EGF addition, supporting the model of a self‐inhibited configuration of the inactive receptor in quiescent cells.
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The snRNP 15.5K protein folds its cognate K-turn RNA: A combined theoretical and biochemical study
TL;DR: A protein-assisted RNA folding mechanism in which the RNA intrinsic flexibility functions as a catalyst is proposed, and it is found that the RNA is significantly more flexible in the absence of the 15.5K protein.
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A parallel stranded linear DNA duplex incorporating dG.dC base pairs.
TL;DR: Based on energy minimizations of a ps-[d(T5GA5).d(A5CT5)] duplex using force field calculations, a model for the conformation of a trans dG.dC base pair in a ps helix is proposed.