Researchers from Duke University Discuss Findings in Essential Amino Acids (Thermodynamic Analysis of Protein Folding and Stability Using a Tryptophan Modification Protocol)
By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators discuss new findings in Essential Amino Acids. According to news originating from Durham, North Carolina, by NewsRx correspondents, research stated, "Described here is the development of a mass spectrometry-based covalent labeling protocol that utilizes the reaction of dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide (HNSB) with tryptophan (Tip) residues to measure protein folding free energies ( Delta G(f) values). In the protocol, the chemical denaturant dependence of the rate at which globally protected Tip residues in a protein react with HNSB is evaluated using either a matrix assisted laser desorption ionization time-of-flight analysis of the intact protein or a quantitative, bottom-up proteomics analysis using isobaric mass tags."
Our news journalists obtained a quote from the research from Duke University, "In the proof-of-principle studies performed here, the protocol yielded accurate Delta G(f) values for the two-state folding proteins, lysozyme and cytochrome c. The protocol also yielded an accurate measure of the dissociation constant (K-d value) for the binding of N,N',N''-triacetylchitotriose to lysozyme, and it successfully detected the binding of brinzolarnide to BCA II, a non-two-state folding protein. The HNSB protocol can be used in combination with SPROX (stability of proteins from rates of oxidation), a previously reported technique that exploits the hydrogen peroxide oxidation of methionine (Met) residues in proteins to make Delta G(f) value measurements. Incorporating the HNSB protocol into SPROX increased the peptide and protein coverage in proteome-wide SPROX experiments by 50% and 25%, respectively."
According to the news editors, the research concluded: "As part of this work, the precision of proteorne-wide Delta G(f) value measurements using the combined HNSB and SPROX protocol is also evaluated."
For more information on this research see: Thermodynamic Analysis of Protein Folding and Stability Using a Tryptophan Modification Protocol. Analytical Chemistry, 2014;86(14):7041-7048. Analytical Chemistry can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Analytical Chemistry - www.pubs.acs.org/journal/ancham)
The news correspondents report that additional information may be obtained from Y.R. Xu, Duke University, Dept. of Chem, Durham, NC 27708, United States. Additional authors for this research include E.C. Strickland and M.C. Fitzgerald (see also Essential Amino Acids).
Keywords for this news article include: Durham, Lysozyme, Tryptophan, United States, North Carolina, Aromatic Amino Acids, Essential Amino Acids, North and Central America
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