Salt bridge: Difference between revisions

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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/2'>hydrogen bonds</scene>.

Myoglobin is an exceptionally soluble protein studded with charged amino acids on its surface. While some of these charged amino acids form saltbridges (here are <scene name='86/864724/Myoglobin_saltbridge/1'>two textbook examples</scene>[https://books.google.com/books?id=gOUsEAAAQBAJ&pg=PA161&lpg=PA161&dq=About+75%25+of+the+charged+residues+in+proteins+are+members+of+ion+pairs+that+are+located+mostly+on+the+protein+surface+(Fig.+6-36)&source=bl&ots=WjtxPwjy2z&sig=ACfU3U2UyRsnSINAhJESbkF84ZZFGpmoVA&hl=en&sa=X&ved=2ahUKEwjkt_mP3qn0AhUSTTABHX9sD_oQ6AF6BAgCEAM#v=onepage&q=About%2075%25%20of%20the%20charged%20residues%20in%20proteins%20are%20members%20of%20ion%20pairs%20that%20are%20located%20mostly%20on%20the%20protein%20surface%20(Fig.%206-36)&f=false]), <scene name='86/864724/Myoglobin_saltbridges/2'>others</scene> do not.

</StructureSection>

== References ==

Salt bridge: Difference between revisions

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 <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/2'>hydrogen bonds</scene>.
+Myoglobin is an exceptionally soluble protein studded with charged amino acids on its surface. While some of these charged amino acids form saltbridges (here are <scene name='86/864724/Myoglobin_saltbridge/1'>two textbook examples</scene>[https://books.google.com/books?id=gOUsEAAAQBAJ&pg=PA161&lpg=PA161&dq=About+75%25+of+the+charged+residues+in+proteins+are+members+of+ion+pairs+that+are+located+mostly+on+the+protein+surface+(Fig.+6-36)&source=bl&ots=WjtxPwjy2z&sig=ACfU3U2UyRsnSINAhJESbkF84ZZFGpmoVA&hl=en&sa=X&ved=2ahUKEwjkt_mP3qn0AhUSTTABHX9sD_oQ6AF6BAgCEAM#v=onepage&q=About%2075%25%20of%20the%20charged%20residues%20in%20proteins%20are%20members%20of%20ion%20pairs%20that%20are%20located%20mostly%20on%20the%20protein%20surface%20(Fig.%206-36)&f=false]), <scene name='86/864724/Myoglobin_saltbridges/2'>others</scene> do not.
 </StructureSection>
 == References ==
 <references/>