A
Aichun Dong
Researcher at University of Northern Colorado
Publications - 22
Citations - 2045
Aichun Dong is an academic researcher from University of Northern Colorado. The author has contributed to research in topics: Infrared spectroscopy & Circular dichroism. The author has an hindex of 18, co-authored 22 publications receiving 1735 citations. Previous affiliations of Aichun Dong include University of Colorado Boulder & Anschutz Medical Campus.
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Journal ArticleDOI
Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy
TL;DR: The principles that underlie the determination of protein secondary structure by FTIR spectroscopy are detailed, as well as the basic steps involved in protein sample preparation, instrument operation,FTIR spectra collection and spectra analysis in order to estimate protein secondary-structural components in aqueous solution.
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IgG particle formation during filling pump operation: a case study of heterogeneous nucleation on stainless steel nanoparticles.
Anil K. Tyagi,Theodore W. Randolph,Aichun Dong,Maloney Kevin,Carl Hitscherich,John F. Carpenter +5 more
TL;DR: It is shown that nanoparticles of foreign materials shed by pumps can serve as heterogeneous nuclei for formation of protein microparticles in a formulation of an IgG.
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Application of infrared spectroscopy to development of stable lyophilized protein formulations.
TL;DR: With infrared spectroscopy it is now possible to examine directly the secondary structure of a protein in the initial aqueous solution, and in both the frozen state and the final dried solid, and it is documented that both freezing and dehydration can induce protein unfolding.
Journal ArticleDOI
Effects of sucrose on conformational equilibria and fluctuations within the native-state ensemble of proteins
Yong Sung Kim,LaToya S. Jones,Aichun Dong,Brent S. Kendrick,Byeong S. Chang,Mark C. Manning,Theodore W. Randolph,John F. Carpenter +7 more
TL;DR: Results indicate that the presence of Sucrose shifts the conformational equilibria toward the most compact protein species within native‐state ensembles, which can be explained by preferential exclusion of sucrose from the protein surface.
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Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution.
Aichun Dong,Brent S. Kendrick,Lotte Kreilgård,James E. Matsuura,Mark C. Manning,John F. Carpenter +5 more
TL;DR: The secondary structure and thermal denaturation (in H2O vs D2O) of recombinant human factor XIII in aqueous solutions were investigated using infrared and circular dichroism (CD) spectroscopies, indicating the presence of a predominantly beta-sheet structure.