about
RNA tertiary interactions mediate native collapse of a bacterial group I ribozymeDynamics of biological macromolecules: not a simple slaving by hydration water.Molecular crowding stabilizes folded RNA structure by the excluded volume effect.Multistage collapse of a bacterial ribozyme observed by time-resolved small-angle X-ray scattering.Molecular crowding overcomes the destabilizing effects of mutations in a bacterial ribozyme.Cooperative tertiary interaction network guides RNA folding.Crowders perturb the entropy of RNA energy landscapes to favor folding.Dynamics of tRNA at different levels of hydration.Metal ion dependence of cooperative collapse transitions in RNASelf-assembled block copolymer photonic crystal for selective fructose detection.Compaction of a bacterial group I ribozyme coincides with the assembly of core helices.Color changing block copolymer films for chemical sensing of simple sugars.Morphotropic phase boundaries in ferromagnets: Tb(1-x)Dy(x)Fe2 alloys.The dynamics of unfolded versus folded tRNA: the role of electrostatic interactions.Effects of Preferential Counterion Interactions on the Specificity of RNA FoldingDynamic Transition in tRNA is Solvent InducedPersistence Length Changes Dramatically as RNA FoldsA nanofluidic ion regulation membrane with aligned cellulose nanofibersThe collapse of free polymer chains in a networkHexagonally ordered nanoparticles templated using a block copolymer film through Coulombic interactionsCellulose ionic conductors with high differential thermal voltage for low-grade heat harvestingMolecular partitioning in ternary solutions of cellulose
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description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Robert M Briber
@ast
Robert M Briber
@en
Robert M Briber
@es
Robert M Briber
@nl
Robert M Briber
@sl
type
label
Robert M Briber
@ast
Robert M Briber
@en
Robert M Briber
@es
Robert M Briber
@nl
Robert M Briber
@sl
prefLabel
Robert M Briber
@ast
Robert M Briber
@en
Robert M Briber
@es
Robert M Briber
@nl
Robert M Briber
@sl
P1053
A-3588-2012
P106
P21
P31
P3829
P496
0000-0002-8358-5942