Abstract
AbstractThe front cover artwork is provided by the group of Prof. D. Flemming Hansen at University College London. The cover illustrates a new NMR method to characterise functional interactions formed by arginine side‐chains. A free side‐chain (fast exchange) and one engaged in a salt‐bridge (slow exchange) are shown. Read the full text of the Article at 10.1002/cphc.201800598.
Highlights
Method to quantify the hydrogen exchange rates of arginine side-chain 1He protons and present a method to gauge the strength of arginine side-chain interactions
An application to the protein T4 Lysozyme is shown, where protection factors calculated from the obtained exchange rates correlate well with the interactions observed in the crystal structure
The method provides a means to quantify the interactions formed by the guanidinium group of arginine sidechains in proteins
Summary
It is important to note that a 90ox 1H pulse followed by the gradient pulse g1 is inserted before the initial recovery delay to ensure that the amount of 1He magnetisation present at the start of each transient is independent of the mixing time, tmix. The 15N 1808 frequency selective pulse (R) is applied with a REBURP shape (3.75 ms at 18.8 T). Proton decoupling during the indirect chemical shift period and during acquisition is achieved with a 4 kHz WALTZ-64[34] scheme.
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