F
Francisco Rodríguez-Ropero
Researcher at Technische Universität Darmstadt
Publications - 44
Citations - 1261
Francisco Rodríguez-Ropero is an academic researcher from Technische Universität Darmstadt. The author has contributed to research in topics: Thiophene & Solvation shell. The author has an hindex of 16, co-authored 44 publications receiving 1125 citations. Previous affiliations of Francisco Rodríguez-Ropero include Polytechnic University of Catalonia & RWTH Aachen University.
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Journal ArticleDOI
Systematic coarse-graining methods for soft matter simulations - a review
Emiliano Brini,Elena A. Algaer,Pritam Ganguly,Chunli Li,Francisco Rodríguez-Ropero,Nico F. A. van der Vegt +5 more
TL;DR: A selected number of applications are discussed as well as limitations of the models and remaining challenges in developing representative and transferable pair potentials inMultiscale modelling of soft matter.
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Mechanism of Polymer Collapse in Miscible Good Solvents.
TL;DR: This work proposes a physical mechanism for co-nonsolvency of a stimulus-responsive polymer in water/methanol mixed solution based on results obtained with molecular simulations and shows that at low alcohol content of the solution methanol preferentially binds to the PNiPAM globule and drives polymer collapse.
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Direct Osmolyte–Macromolecule Interactions Confer Entropic Stability to Folded States
TL;DR: This work discusses poly(N-isopropylacrylamide) (PNiPAM) in water whose folding/unfolding equilibrium shifts toward the folded state in the presence of urea, and proposes a new microscopic mechanism that explains how direct osmolyte-macromolecule interactions confer stability to folded states.
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Cloning and characterization of a thermostable and halo-tolerant endoglucanase from Thermoanaerobacter tengcongensis MB4
Chaoning Liang,Yanfen Xue,Marco Fioroni,Francisco Rodríguez-Ropero,Cheng Zhou,Ulrich Schwaneberg,Yanhe Ma +6 more
TL;DR: A β-1,4-endoglucanase cloned from the genomic DNA of saccharolytic thermophilic eubacterium Thermoanaerobacter tengcongensis MB4 and functionally expressed in Escherichia coli exhibits high residual activities in molar concentration of NaCl and KCl, and is remarkably resistant in ionic liquids.
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Directed evolution of a thermophilic endoglucanase (Cel5A) into highly active Cel5A variants with an expanded temperature profile.
Chaoning Liang,Marco Fioroni,Francisco Rodríguez-Ropero,Yanfen Xue,Ulrich Schwaneberg,Yanhe Ma +5 more
TL;DR: Molecular Dynamics simulations performed on the 3F6 and C3-13 variants show a decreased number of intra-Cel5A hydrogen bonds compared to the wild type, implying a more flexible protein skeleton which correlates well to the higher catalytic activity at lower temperatures.