Signatures of co-translational folding.
Global and co-translational protein folding may both occur in vivo, and understanding the relationship between these folding mechanisms is pivotal to our understanding of protein-structure formation. Within this study, over 1.5 million hydrophobic-polar sequences were classified based on their abili...
| Autores principales: | , , |
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| Formato: | Journal article |
| Lenguaje: | English |
| Publicado: |
2011
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| _version_ | 1826260791561551872 |
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| author | Saunders, R Mann, M Deane, C |
| author_facet | Saunders, R Mann, M Deane, C |
| author_sort | Saunders, R |
| collection | OXFORD |
| description | Global and co-translational protein folding may both occur in vivo, and understanding the relationship between these folding mechanisms is pivotal to our understanding of protein-structure formation. Within this study, over 1.5 million hydrophobic-polar sequences were classified based on their ability to attain a unique, but not necessarily minimal energy conformation through co-translational folding. The sequence and structure properties of the sets were then compared to elucidate signatures of co-translational folding. The strongest signature of co-translational folding is a reduced number of possible favorable contacts in the amino terminus. There is no evidence of fewer contacts, more local contacts, or less-compact structures. Co-translational folding produces a more compact amino- than carboxy-terminal region and an amino-terminal-biased set of core residues. In real proteins these signatures are also observed and found most strongly in proteins of the alpha/beta structural class of proteins (SCOP) where 71 % have an amino-terminal set of core residues. The prominence of co-translational features in experimentally determined protein structures suggests that the importance of co-translational folding is currently underestimated. |
| first_indexed | 2024-03-06T19:11:20Z |
| format | Journal article |
| id | oxford-uuid:16def939-3e82-4efa-a238-05940f19fda0 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:11:20Z |
| publishDate | 2011 |
| record_format | dspace |
| spelling | oxford-uuid:16def939-3e82-4efa-a238-05940f19fda02022-03-26T10:33:54ZSignatures of co-translational folding.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:16def939-3e82-4efa-a238-05940f19fda0EnglishSymplectic Elements at Oxford2011Saunders, RMann, MDeane, CGlobal and co-translational protein folding may both occur in vivo, and understanding the relationship between these folding mechanisms is pivotal to our understanding of protein-structure formation. Within this study, over 1.5 million hydrophobic-polar sequences were classified based on their ability to attain a unique, but not necessarily minimal energy conformation through co-translational folding. The sequence and structure properties of the sets were then compared to elucidate signatures of co-translational folding. The strongest signature of co-translational folding is a reduced number of possible favorable contacts in the amino terminus. There is no evidence of fewer contacts, more local contacts, or less-compact structures. Co-translational folding produces a more compact amino- than carboxy-terminal region and an amino-terminal-biased set of core residues. In real proteins these signatures are also observed and found most strongly in proteins of the alpha/beta structural class of proteins (SCOP) where 71 % have an amino-terminal set of core residues. The prominence of co-translational features in experimentally determined protein structures suggests that the importance of co-translational folding is currently underestimated. |
| spellingShingle | Saunders, R Mann, M Deane, C Signatures of co-translational folding. |
| title | Signatures of co-translational folding. |
| title_full | Signatures of co-translational folding. |
| title_fullStr | Signatures of co-translational folding. |
| title_full_unstemmed | Signatures of co-translational folding. |
| title_short | Signatures of co-translational folding. |
| title_sort | signatures of co translational folding |
| work_keys_str_mv | AT saundersr signaturesofcotranslationalfolding AT mannm signaturesofcotranslationalfolding AT deanec signaturesofcotranslationalfolding |