Protein arrays fabrication have been extensively used in the bio-sensing and bio-analysis applications. A key issue in the array technology is to transduce the recognition events to readable signals. In our previous work, 1-Cysteine-mutated calmodulin (CaM) was immobilization on a mercapto-terminated surface through cysteine-Hg-mercapto coupling. Its conformational change was characterized via Atomic Force Microscopy (AFM). In this study, Kelvin Probe Force Microscopy (KPFM), which can measure surface potential variations during a reaction, was utilized to detect the conformational change of CaM to Apo-CaM. Through KPFM characterization, it was also found that the immobilized CaM has two different orientations. This orientational difference might have an influence on the efficiency and robustness of immobilized CaM on a surface. Our results demonstrated that KPFM was capable of detecting the protein conformational change, as well as probing the protein orientational difference.Reference: 1. Trajkovic, S.; Zhang, X.  ; Daunert, S.; Cai, Y.  Langmuir 2011  .

Kelvin probe force microscopy (KPFM) study of the conformational change and orientational difference in immobilized calmodulin (CaM)

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.