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  Ligand binding: Molecular mechanics calculation of the streptavidin-biotin rupture force.

Grubmüller, H., Heymann, B., & Tavan, P. (1996). Ligand binding: Molecular mechanics calculation of the streptavidin-biotin rupture force. Science, (5251), 997-999. doi:10.1126/science.271.5251.997.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-CA21-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C4A6-0
Genre: Journal Article

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 Creators:
Grubmüller, H.1, Author              
Heymann, B., Author
Tavan, P., Author
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1Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              

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 Abstract: The force required to rupture the streptavidin-biotin complex was calculated here by computer simulations. The computed force agrees well with that obtained by recent single molecule atomic force microscope experiments. These simulations suggest a detailed multiple-pathway rupture mechanism involving five major unbinding steps. Binding forces and specificity are attributed to a hydrogen bond network between the biotin ligand and residues within the binding pocket of streptavidin. During rupture, additional water bridges substantially enhance the stability of the complex and even dominate the binding interactions. In contrast, steric restraints do not appear to contribute to the binding forces, although conformational motions were observed.

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Language(s): eng - English
 Dates: 1996
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.271.5251.997
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: (5251) Sequence Number: - Start / End Page: 997 - 999 Identifier: ISSN: 0036-8075