Angela M. Bardo

ORCID: 0000-0002-6637-4748
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About
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Research Areas
  • Advanced biosensing and bioanalysis techniques
  • Photochemistry and Electron Transfer Studies
  • Advanced Proteomics Techniques and Applications
  • Click Chemistry and Applications
  • Analytical Chemistry and Sensors
  • Advanced Fluorescence Microscopy Techniques
  • Gene expression and cancer classification
  • Spectroscopy and Quantum Chemical Studies
  • Aerogels and thermal insulation
  • Molecular Biology Techniques and Applications
  • Advanced Biosensing Techniques and Applications
  • Surface Modification and Superhydrophobicity
  • Supramolecular Self-Assembly in Materials
  • RNA modifications and cancer
  • Glycosylation and Glycoproteins Research
  • RNA and protein synthesis mechanisms
  • Single-cell and spatial transcriptomics
  • Porphyrin and Phthalocyanine Chemistry
  • Nonlinear Optical Materials Studies
  • Cancer Genomics and Diagnostics
  • Monoclonal and Polyclonal Antibodies Research
  • Photonic Crystals and Applications
  • Mesoporous Materials and Catalysis

The University of Texas at Austin
2018-2024

Kansas State University
1998-2002

Single molecule spectroscopic methods are used to obtain detailed information on the polarity and rigidity of molecular-scale environments found in thin poly(vinyl alcohol) (PVA) poly(methyl methacrylate) (PMMA) films. Nile Red is employed as a highly sensitive probe environmental properties these experiments. Fluorescence spectra recorded for numerous single molecules their peak positions widths determined by fitting Gaussian functions. The spectral data analyzed using new model dependence...

10.1021/jp992312y article EN The Journal of Physical Chemistry B 1999-12-23

The practical application of new single molecule protein sequencing (SMPS) technologies requires accurate estimates their associated error rates. Here, we describe the development and two distinct parameter estimation methods for analyzing SMPS reads produced by fluorosequencing. A Hidden Markov Model (HMM) based approach, extends whatprot, where previously used HMMs peptide-read matching. This extension offers a principled approach estimating key parameters fluorosequencing experiments,...

10.1371/journal.pcbi.1012258 article EN cc-by PLoS Computational Biology 2024-07-05

Single molecule confocal microspectroscopic methods are used to characterize individual molecular-scale environments in silicate thin films for the first time. Rhodamine dyes doped into materials at nanomolar levels as probes of physicochemical environment which each is entrapped. The results compared those obtained from dye-doped organic polymer films. Static fluorescence spectra and time-dependent signals recorded a large number single molecules show be highly inhomogeneous comparison...

10.1021/jp982574k article EN The Journal of Physical Chemistry B 1998-08-20

Single-molecule fluorescence spectroscopy is used to compare the nanoscale properties of organically modified sol−gel-derived silicate thin films prepared from different precursors. Sols containing mole fractions isobutyltrimethoxysilane (BTMOS) and/or 3-(triethoxysilyl)propionitrile (CNS) and tetraethoxysilane (TEOS) are for film preparation. The solvent-sensitive dye Nile red doped into these at nanomolar concentrations probe their environments. single-molecule spectra obtained analyzed...

10.1021/cm020344j article EN Chemistry of Materials 2002-07-26

The nanoscale properties of organically modified sol−gel-derived silicate thin films are studied in detail by single-molecule spectroscopic methods. For these studies, the solvent-sensitive probe Nile Red is doped into at nanomolar concentrations. Spectroscopic data obtained for prepared from sols containing different mole fractions isobutyltrimethoxysilane and tetraethoxysilane. analyzed using a model based on Marcus theory, providing important new information static local film such as...

10.1021/cm010296n article EN Chemistry of Materials 2001-07-10

Single-molecule spectroscopy is used to characterize the microenvironments found in silicate thin films dried under different conditions. Local film properties are assigned on basis of fluorescence emission characteristics individual dopant (rhodamine B) molecules. The samples studied include those characterized immediately after being spin cast onto a glass substrate (fresh samples) and drying at ≈80 °C vacuum oven for least 12 h (dried samples). single-molecule spectra shift red more...

10.1021/jp001011h article EN The Journal of Physical Chemistry B 2000-10-10

The field of proteomics has expanded recently with more sensitive techniques for the bulk measurement peptides as well single-molecule techniques. One limiting factor some these methods is need multiple chemical derivatizations and highly pure proteins free contaminants. We demonstrate a solid-phase capture-release strategy suitable proteolysis, purification, subsequent modification peptides. use this resin on an HEK293T cell lysate perform one-pot capture, derivatization to survey peptide...

10.1021/acschembio.0c00040 article EN ACS Chemical Biology 2020-05-02

ABSTRACT The need to accurately survey proteins and their modifications with ever higher sensitivities, particularly in clinical settings limited samples, is spurring development of new single molecule proteomics technologies. Fluorosequencing one such highly parallelized peptide sequencing platform, based on determining the sequence positions select amino acid types within peptides enable identification quantification from a reference database. Here, we describe substantial improvements...

10.1101/2023.09.15.558007 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-09-16

A peptide sequencing scheme utilizing fluorescence microscopy and Edman degradation to determine the amino acid position in fluorophore-labeled peptides was recently reported, referred as fluorosequencing. It observed that multiple fluorophores covalently linked a scaffold resulted decrease anticipated output worsened single-molecule analysis. In this study, we report an improvement photophysical properties of by incorporating long flexible (PEG)

10.1021/acs.bioconjchem.2c00103 article EN Bioconjugate Chemistry 2022-05-27

The practical application of new single molecule protein sequencing (SMPS) technologies requires accurate estimates their associated error rates. Here, we describe the development and two distinct parameter estimation methods for analyzing SMPS reads produced by fluorosequencing. A Hidden Markov Model (HMM) based approach, extends

10.1101/2023.07.18.549591 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2023-07-19

Silica passivating agents have shown great success in minimizing nonspecific protein binding to glass surfaces for imaging and microscopy applications. Amine-derivatized are commonly used conjugation with amide coupling immobilize peptides/proteins through C-terminal or side-chain carboxylic acids. In the case of single-molecule fluorosequencing peptides, attachment occurs via C-terminus surface has previously been a source error peptide identification. Here, we employ as high-throughput,...

10.1021/acs.langmuir.1c02644 article EN Langmuir 2021-12-14

ADVERTISEMENT RETURN TO ISSUEPREVAddition/CorrectionORIGINAL ARTICLEThis notice is a correctionNanoscale Properties and Matrix−Dopant Interactions in Dye-Doped Organically Modified Silicate Thin Films.Angela M. Bardo, Maryanne Collinson, Daniel A. HigginsCite this: Chem. Mater. 2001, 13, 9, 3058Publication Date (Web):August 22, 2001Publication History Published online22 August 2001Published inissue 1 September...

10.1021/cm012009l article EN Chemistry of Materials 2001-08-22

Abstract The field of proteomics has expanded recently with more sensitive techniques for the bulk measurement peptides as well single-molecule techniques. One limiting factor some these methods is need multiple chemical derivatizations and highly pure proteins free contaminants. We demonstrate a solid-phase capture strategy suitable proteolysis, purification, subsequent modification peptides. use this resin on an HEK293T cell lysate perform one-pot capture, derivatization to generate...

10.1101/2020.01.13.904540 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-01-14
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