Ultrafast solvation dynamics at internal sites of staphylococcal nuclease investigated by site-directed mutagenesis<xref ref-type="fn" rid="cpb142543fn1">*</xref>

Ultrafast solvation dynamics at internal sites of staphylococcal nuclease investigated by site-directed mutagenesis*

Gao Guang-Yu^a), Li Yu^a), Wang Wei^a), Wang Shu-Feng^a)†, Dongping Zhong^b), Gong Qi-Huang^a),^c)

Fig. 2. a X-ray of the crystal structure of SNase PDB:1SNO. The positions where Trp is substituted are denoted by purple sticks, i.e., positions 34, 36, 38, and 41. b Active region of SNase, shown in surface mode, where the substrate analogue, pdTp, and ligand Ca 2#cod#x002B; are inserted to demonstrate the two binding pockets, shown by sticks.