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We describe a methodology to perform reliable tunneling spectroscopy in electrochemical media. Sequential in situ tunneling spectra are recorded while the electrochemical potential of the electrode is scanned. Spectroscopic data are presented as conductance maps or conductograms that show the in situ electronic structure of an electrode surface while it undergoes an electrochemical reaction. The conductance map or conductogram represents the redox fingerprint of an electrode/liquid interface in a specific medium and can serve to predict its electrochemical behavior in a quantitative energy scale. The methodology is validated studying the reversible oxidation and passivity of an iron electrode in borate buffer, and we describe the main quantitative information that can be extracted concerning the semiconducting properties of the Fe passive film. This methodology is useful to study heterogeneous catalysis, electrochemical sensing and bioelectronic systems.

We present a new procedure to prepare Pt/Ir probes for electrochemical scanning tunneling microscopy (STM) and spectroscopy applications. We detail the experimental setup and the improvements over previous methods. The probes have been used successfully for measurements of tunneling spectroscopy under electrochemical control, which requires scanning the potential of the tip at high velocity.

The RNA binding characteristics of wild-type and deletion constructs of polypyrimidine tract binding protein that have RNA recognition motifs in both an oligomeric and monomeric context were examined to correlate structural motifs with their roles. Results showed that there is no strong correlation between the RNA binding affinity and specificity upon oligomerization. However, the mode of RNA interaction and dimerization is related.

The scanning tunneling microscope break junction technique is employed to explain the various transport characteristics that are exhibited by the long conjugated molecular wires. The impact of the length and the temperature on the conductance behavior of these wires is also analyzed.

The oxidation and reduction processes of both polycrystalline tin and Sn (100) single crystals are investigated in borate buffer solution of pH 7.5 using cyclic voltammetry and in-situ characterizations such as Raman scattering, potential modulated reflectance spectroscopy (PMRS), and electrochemical scanning tunneling microscopy (EC-STM).

Amyloids are a family of self-aggregating proteins implicated in various central nervous system disorders, including Alzheimer's disease (AD). It is thought that prefibrillar soluble forms of amyloid peptides, including oligomers, may be the main pathogenic factor in AD. Herein we describe the fabrication of well-defined, functionalized, monomeric beta-amyloid peptide surfaces for studying protein-protein interactions. We first prepared a nonaggregating analogue of the beta-amyloid peptide and then attached it to a gold surface covered with a self-assembled monolayer (SAM) of alkanethiols. After attachment, the native form of the beta-amyloid peptide (Abeta40) was obtained by surface-level intramolecular O-N migration. The surface was characterized by atomic force microscopy (AFM) and self-assembled monolayer for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (SAMDI-TOF MS). The interaction between the surface-bound Abeta40 and monoclonal anti-Abeta40 antibody was tracked by AFM and chemiluminescence, which revealed that the Abeta40 was attached mainly in its monomeric form and that the protein-protein complex was assembled on the surface. Last, we used a proteomics approach to demonstrate the specificity of the Abeta40-functionalized surface in surface-binding experiments employing serum amyloid P (SAP) and bovine serum albumin (BSA).