László Grama
University of Pécs
22 Papers
385 Citations
László Grama is an academic researcher from University of Pécs. The author has contributed to research in topics: Titin & Chemistry. The author has an hindex of 13, co-authored 22 publications. Previous affiliations of László Grama include Hungarian Academy of Sciences.
Chat about Author
Papers
Reversible Mechanical Unzipping of Amyloid β-Fibrils
Miklós S.Z. Kellermayer,László Grama,Árpád Karsai,Attila Nagy,Amram Kahn,Zsolt László Datki,Botond Penke +6 more
TL;DR: The rapid, cooperative zipping together of β-sheets could be an important mechanism behind the self-assembly of amyloid fibrils, and the repetitive force patterns contribute to a mechanical fingerprint that could be utilized in the characterization of different amyloidsfibrils.
91
Differential actin binding along the PEVK domain of skeletal muscle titin.
Attila Nagy,Paola Cacciafesta,László Grama,András Kengyel,András Málnási-Csizmadia,Miklós S.Z. Kellermayer +5 more
TL;DR: A differential actin binding is found along PEVK in solid-state binding, cross-linking and in vitro motility assays, suggesting that a local preponderance of polyE motifs conveys an enhanced local actin-binding property to PEVK.
Spatially and Temporally Synchronized Atomic Force and Total Internal Reflection Fluorescence Microscopy for Imaging and Manipulating Cells and Biomolecules
Miklós S.Z. Kellermayer,Árpád Karsai,András Kengyel,Attila Nagy,Pasquale Bianco,Tamás Huber,Ágnes Kulcsár,Csaba Niedetzky,Roger Proksch,László Grama +9 more
TL;DR: It is demonstrated that with the technique, correlated sample topography and fluorescence images can be recorded, soft biomolecular systems can be mechanically manipulated in a targeted fashion, and the fluorescence of mechanically stretched titin can be followed with high temporal resolution.
60
Hierarchical Extensibility in the PEVK Domain of Skeletal-Muscle Titin
Attila Nagy,László Grama,Tamás Huber,Pasquale Bianco,Karoly Trombitás,Henk Granzier,Miklós S.Z. Kellermayer +6 more
TL;DR: The effective persistence lengths decreased as a function of ionic strength, as predicted by the Odijk-Skolnick-Fixman model of polyelectrolyte chains, indicating that the residual differences in the elasticity of the segments derive from nonelectrostatic mechanisms.
58
Mechanical manipulation of Alzheimer’s amyloid β1–42 fibrils
TL;DR: It is shown that Aβ-subunit sheets can be mechanically unzipped from the fibril surface with constant forces in a reversible transition, and the nanomechanical fingerprint of the Aβ1–42 is further influenced by the structural dynamics of intrafibrillar interactions.
56