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  Force spectroscopy of single biomolecules.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F411-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E556-F
Genre: Journal Article

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 Creators:
Rief, M., Author
Grubmueller, H.1, Author              
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1Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578630              

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Free keywords: atomic force microscopy; molecular dynamics simulations; molecular recognition; protein folding; single molecules
 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.

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Language(s): eng - English
 Dates: 2002-03-12
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: ChemPhysChem
Source Genre: Journal
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Pages: - Volume / Issue: 3 (3) Sequence Number: - Start / End Page: 255 - 261 Identifier: -