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Journal Article

Force spectroscopy of single biomolecules.

MPS-Authors
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Grubmueller,  H.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

599666.pdf
(Publisher version), 238KB

Supplementary Material (public)

599666_1.pdf
(Supplementary material), 19KB

Citation

Rief, M., & Grubmueller, H. (2002). Force spectroscopy of single biomolecules. ChemPhysChem, 3(3), 255-261. Retrieved from http://onlinelibrary.wiley.com/doi/10.1002/1439-7641(20020315)3:3%3C255:AID-CPHC255%3E3.0.CO;2-M/pdf.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F411-2
Abstract
Many processes in the body are effected and regulated by highly, specialized protein molecules: These molecules certainly deserve name "biochemical nonomachines". Recent progress in single-molecule experiments and corresponding simulations with super,computers enable us to watch these "nanomachines" at work, revealing a host of astounding mechanisms. Examples are the fine-tuned movements of the binding pocket of a receptor protein,locking into its ligand molecule and the forced unfolding of titin, which acts as a molecular shock absorber to protect muscle cells. At present, we are not capable of designing such high precision machines, but we are beginning to understand their working principles and to simulate and predict their function.