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Full-Text Articles in Chemistry
Double Cysteine Mutations In Staphylococcal Nuclease: The Effect Of Artificially Introduced Disulfide Bonds On Protein Structure And Stability, Anna Terry
Inquiry: The University of Arkansas Undergraduate Research Journal
Since a protein's function depends on its structure, basic research in protein structure facilitates the solution of many practical problems, such as the synthesis of more effective medicines. With this larger goal in sight, the purpose of this research project is to understand better the chemical principles that underlie protein structure and stability. Disulfide bonds are a potentially stabilizing feature of many proteins. They may form between cysteine residues in close proximity to one another if the orientation is favorable. Often found in proteins produced by organisms that grow at high temperatures, disulfide bonds may anchor side chains together, making …
Studies Of Tryptophans In Membrane- Spanning "Walp" Peptides By Deuterium Nmr Spectroscopy, Nichole Reed
Studies Of Tryptophans In Membrane- Spanning "Walp" Peptides By Deuterium Nmr Spectroscopy, Nichole Reed
Inquiry: The University of Arkansas Undergraduate Research Journal
WALP pep tides of sequence acetyl-Gly-Trp-Trp-(Leu-Ala)-Trp-Trp-Ala-ethanolamine insert into lipid bilayers as membrane-spanning a-helices and modulate the lipid phase behavior as functions of n and the lipid acyl chain length. A key feature of the WALP peptides is the positioning of tryptophan (Trp) indole rings at the membrane/water interface. For the examples WALP19 with n = 6.5 and WALP23 with n = 8.5, we have labeled individual indoles with deuterium and incorporated the labeled peptides in oriented, hydrated bilayers of Dimyristoyl-phosphatidylcholine (DMPC). Deuterium NMR spectra from these samples show sharp resonances when the membrane normal is aligned either parallel (Beta = …