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Electrostatics can alter the RNA-binding properties of proteins that display structure selectivity without sequence specificity. Loquacious-PD relies on this broad scope response to mediate the interaction of endonucleases with double stranded RNAs. Multimodal spectroscopic probes with in situ perturbations reveal an efficient and stable binding mechanism that disfavors high protein density complexes and is sensitive to local electrostatics. 

Abstract The dynamic conformations of a thin peptide film covalently‐linked to the surface of a transparent electrode are characterized over the course of a perturbation to their local pH by a photoacid under a controlled electrostatic potential. The local environment at this functionalized electrified interface is probed by the ultrafast fluorescence intensity and transient anisotropy of chromophores sparsely attached to the peptide side chains. A partition of chromophores into two sub‐populations is observed, one buried in the peptide layer and another that is solvent exposed, and their relative contributions to the observed fluorescence signal are affected by both pH and voltage stimuli. The photophysical properties of solvent‐exposed chromophores reveal that while the average conformation of the peptide mat is dictated by the pH of the surrounding electrolyte, their fluctuations are largely determined by the local electrostatic conditions set by the electrode's surface potential. 

The complex and dynamic interfacial regions between biological samples and electronic components pose many challenges for characterization, including their evolution over multiple temporal and spatial scales. Spectroscopic probes of buried interfaces employing mid-infrared plasmon resonances and time-resolved fluorescence detection in the visible range are used to study the properties of polypeptides adsorbed at the surface of a working electrode. Information from these complementary spectroscopic probes reveals the interplay of solvation, electric fields, and ion concentration on their resulting macromolecular conformations.