Salt bridge
From Proteopedia
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==Examples== | ==Examples== | ||
<StructureSection load='4s0w' size='340' side='right' caption='' scene=''> | <StructureSection load='4s0w' size='340' side='right' caption='' scene=''> | ||
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| + | Salt bridges can be classified by <scene name='86/864724/T4_internal/1'>buried</scene> or solvent exposed. They can also be classified by interaction partners, distance of these partner along the primary sequence, geometry of interactions, and patterns with more than two interaction partners<ref>PMID: 21287621</ref>. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:02, 18 October 2020
Salt bridge are ionic interactions between oppositely charged side chains in proteins. Sometimes, interactions between charged side chains and bound ions are also call salt bridges. The strength of a salt bridge is strongly dependent on the chemical environment (solvent exposed or buried, nature of the solvent).
Examples
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References
- ↑ Donald JE, Kulp DW, DeGrado WF. Salt bridges: geometrically specific, designable interactions. Proteins. 2011 Mar;79(3):898-915. doi: 10.1002/prot.22927. Epub 2011 Jan 5. PMID:21287621 doi:http://dx.doi.org/10.1002/prot.22927
