The Florida State University Research Foundation, Inc.

Alan G Marshall

Ryan P Rodgers

Priyanka Juyal

Mark R Emmett

Sasa Kazazic

Michael J Greig

Steven C Beu

Greg T Blakney

John P Quinn

Christopher L Hendrickson

Mmilili M Mapolelo

A method of enhanced speciation of both positive and negatives species in an analyte is disclosed. The method can include producing a first analyte solution comprising an analyte composition and an effective amount of silver triflate, and analyzing the first analyte solution with an electrospray ionization mass spectrometer. The method can also include producing a second analyte solution comprising a portion of the analyte composition and an effective amount of a compound of formula I, and analyzing the second analyte solution with an electrospray ionization mass spectrometer. The compound of formula I is [NX][OH], where X is a linear, branched, or cyclic C-Calkane; an aryl; a heterocyclic aromatic; or a heterocyclic moiety.

Electrospray ionization mass spectrometry methodology

A method for quantifying the presence of naphthenic acids in a hydrocarbon-comprising liquid that includes: contacting a hydrocarbon-comprising liquid with gaseous ammonia; isolating a reaction product produced by the contacting step; and analyzing the reaction product for the presence of naphthenates using a mass spectrometry technique. The naphthenic acids known to form commercial naphthenate deposits can be (i) ions of tetraprotic carboxylic acids having molecular weights ranging from 1225 to 1270 Daltons, (ii) n-alkyl or branched carboxylic acids having molecular weights ranging from 250 to 650 Daltons, or (iii) both.

Method for identifying naphthenates in a hydrocarbon containing liquid

Analytical methods using hydrogen/deuterium exchange are provided which reduce or eliminate the back-exchange of deuterium for hydrogen. The methods, which are useful in protein and peptide mapping, include the steps of (a) providing a peptide or protein comprising a solvent accessible hydrogen; (b) exchanging the solvent accessible hydrogen for a deuterium; (c) separating the peptide or protein with supercritical fluid chromatography; and (d) analyzing by mass spectrometry the mass of the separated peptide or protein. Supercritical fluid chromatography enables the observation of fast exchanging hydrogen atoms missed using conventional liquid chromatography methods.

Analytical method for protein mapping using hydrogen/deuterium exchange

A high resolution Fourier Transform Ion Cyclotron Resonance (FT-ICR) mass spectrometry system includes excitation circuitry including an excitation amplifier for generating an electrical excitation signal and excitation electrodes for applying an oscillating electric field to excite ions in the system. Detection circuitry including detection electrodes measures a detection signal which includes a plurality of signal values including signal values induced by the ions. Structure is provided for reducing or canceling coupling of the excitation signal into the detection signal, wherein simultaneous excitation and detection is used. A computing structure generates a Fourier transformed frequency domain representation of the detection signal and deconvolves the frequency domain representation using complex division to separate a dispersion spectrum portion and an absorption spectrum portion.

High resolution fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry methods and apparatus

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Tallahassee, FL, United States of America

Alan G Marshall