Investigation on the Binding and Conformational Change of All-<i>trans</i>-Retinoic Acid with Peptidyl Prolyl <i>cis</i>/<i>trans</i> Isomerase Pin1 Using Spectroscopic and Computational Techniques

<div>The crystal structure of Pin1 (a) and chemical structure of ATRA (b). W11, W34, and W73 are three tryptophan residues.</div>

Journal of Spectroscopy

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Figure 1: Investigation on the Binding and Conformational Change of All-<i>trans</i>-Retinoic Acid with Peptidyl Prolyl <i>cis</i>/<i>trans</i> Isomerase Pin1 Using Spectroscopic and Computational Techniques 

Figure 1 | Investigation on the Binding and Conformational Change of All-trans-Retinoic Acid with Peptidyl Prolyl cis/trans Isomerase Pin1 Using Spectroscopic and Computational Techniques 