Fig. 1: Experimental results for peptides in SDS micelles. | Communications Chemistry

Fig. 1: Experimental results for peptides in SDS micelles.

From: Probing the dynamic landscape of peptides in molecular assemblies by synergized NMR experiments and MD simulations

Fig. 1

a Amino acid sequences with 15N labelled residues shown in red for transmembrane GWALP23, peripheral Magainin 2, and mitochondria-directed tail anchor (eElaB(TA), eYqjD(TA), yFis1(TA), and hMff(TA)) peptides. b 1H - 15N HSQC spectra and (c) T1, T2 and hetNOE spin relaxation times measured from the peptides in SDS micelle and sodium-phosphate buffer at 310 K with 850 MHz spectrometer.

Back to article page