Stability of Bacteriorhodopsin α-Helices and Loops Analyzed by Single-Molecule Force Spectroscopy

By D. Müller, Max Kessler, F. Oesterhelt, C. Möller, D. Oesterhelt, H. Gaub. 2002

145 citations recorded by the source corpus.

Subfields: Atomic and Molecular Physics, and Optics, Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/f343fcc520574529b441023182e68abdfad49548

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Atomic and Molecular Physics, and Optics

1. Daniel J. Muller
2. Andrea Alessandrini
3. Christian A. Bippes
4. Paolo Facci

In Molecular Biology

1. Daniel J. Muller
2. Christian A. Bippes

Citations in the corpus

• AFM: a versatile tool in biophysics (2005, background): “Also sequential unfolding of transmembrane domains of bacteriorhodopsin embedded in its native purple membrane has been studied, elucidating also the role of pH, temperature and point mutations on the stability of individual transmembrane domains [268].”
• High-resolution atomic force microscopy and spectroscopy of native membrane proteins (2011, background): “Consequently, the interactions stabilizing individual secondary structure elements of membrane proteins have been probed in dependence on temperature [308], pH [309], electrolyte [310], oligomeric state [311] and in the context of protein–protein interactions [312].”