Figure 5 | Scientific Reports

Figure 5

From: Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study

Figure 5

Surface representations of LEN, SMA and the eight SMA-like mutants of LEN in dimer form, depicting the locations of the most dynamic residues. The proteins are arranged in the order of decreasing thermodynamic stability with respect to LEN as reported by Raffen et al.10, with LEN S29N (A) being the most stable and Y96Q (J) the most unstable. The R ex values obtained at 600 MHz 1H frequency are mapped onto the X-ray structure of LEN with color coding similar to that used in Fig. 4.

Back to article page