Salt bridge: Difference between revisions
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<StructureSection load='' size='340' side='right' caption='' scene='86/864724/T4_internal/1'> | <StructureSection load='' size='340' side='right' caption='' scene='86/864724/T4_internal/1'> | ||
Salt bridges can be classified as <scene name='86/864724/Chymotrypsin/2'>buried</scene> or <scene name='86/864724/T4_internal/1'>solvent exposed.</scene> 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>. | Salt bridges can be classified as <scene name='86/864724/Chymotrypsin/2'>buried</scene> or partially <scene name='86/864724/T4_internal/1'>solvent exposed.</scene> 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>. Most salt bridges also show <scene name='86/864724/Amylase/1'>hydrogen bonds</scene>. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 02:05, 19 October 2020
Salt bridges 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). The contribution of salt bridges to the folded state of the protein is complicated [1].
Examples
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References
- ↑ Hendsch ZS, Tidor B. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 1994 Feb;3(2):211-26. doi: 10.1002/pro.5560030206. PMID:8003958 doi:https://dx.doi.org/10.1002/pro.5560030206
