User:Jaime Prilusky/SequenceToStructure
From Proteopedia
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| + | == A one-way street == | ||
| + | A very basic axiom in Structural Bioinformatics states that a protein sequence has all the required information to fold and become a spatial structure. This sounds reasonable as long as a the same protein sequence, with no extra help, always assumes the same three dimensional configuration when folding. No external guidance. No errors. The sequence simply ''knows'' it's final destination. | ||
| + | In summary: multiple copies of the same protein sequence will always fold into the same 3D structure. Different protein sequences will, of course, fold into different spatial conformations. | ||
| + | <br> | ||
| + | This sounds like a clear ''one-way street'' example: from any given protein sequence you can obtain one, and only one structure <ref>There's a long list of known protein structures that present conformational changes, this is, that don't present a single spatial conformation, but a series of possible states. Still the ''one-way stree'' idea holds, because the same protein will always fold into the same moving structure. See the [http://molmovdb.org/ Database of Macromolecular Movements] for examples of conformational changes in proteins' structures</ref>. | ||
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<applet load='T0498.pdb' size='300' frame='true' align='right' caption='T0498' scene='User:Jaime_Prilusky/SequenceToStructure/T0498/1' /> | <applet load='T0498.pdb' size='300' frame='true' align='right' caption='T0498' scene='User:Jaime_Prilusky/SequenceToStructure/T0498/1' /> | ||
| - | <applet load='T0499.pdb' size='300' frame='true' align='right' caption='T0499' scene='User:Jaime_Prilusky/SequenceToStructure/T0499/1' /> | + | <applet load='T0499.pdb' size='300' frame='true' align='right' caption='T0499' scene='User:Jaime_Prilusky/SequenceToStructure/T0499/1' /> |
| - | + | == Let's get folded == | |
| + | Going from an amorphous, unstructured state into a beautiful and complex 3D structure is a trivial routine for a protein sequence: ″''You only need to follow your instinct''″. But for us, external observers, the process is not so obvious, the rules are not so clear, and guessing the final 3D structure from only a protein sequence is a very difficult job. | ||
| + | <br> | ||
| + | Some obvious things we do know: longer protein sequences are associated to larger structures. | ||
| - | + | ||
| + | {{Clear}} | ||
| + | == References == | ||
| + | <references/> | ||
Current revision
A one-way street
A very basic axiom in Structural Bioinformatics states that a protein sequence has all the required information to fold and become a spatial structure. This sounds reasonable as long as a the same protein sequence, with no extra help, always assumes the same three dimensional configuration when folding. No external guidance. No errors. The sequence simply knows it's final destination.
In summary: multiple copies of the same protein sequence will always fold into the same 3D structure. Different protein sequences will, of course, fold into different spatial conformations.
This sounds like a clear one-way street example: from any given protein sequence you can obtain one, and only one structure [1].
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Let's get folded
Going from an amorphous, unstructured state into a beautiful and complex 3D structure is a trivial routine for a protein sequence: ″You only need to follow your instinct″. But for us, external observers, the process is not so obvious, the rules are not so clear, and guessing the final 3D structure from only a protein sequence is a very difficult job.
Some obvious things we do know: longer protein sequences are associated to larger structures.
References
- ↑ There's a long list of known protein structures that present conformational changes, this is, that don't present a single spatial conformation, but a series of possible states. Still the one-way stree idea holds, because the same protein will always fold into the same moving structure. See the Database of Macromolecular Movements for examples of conformational changes in proteins' structures
