Dissociation of the human spliceosomal U1 snRNP complex
The non-covalent interactions which maintain protein-RNA complexes such as U1 snRNP in human spliceosome were investigated using nanoflow ESI-MS technique. The reconstituted U1 snRNP complex comprised core domain of Sm proteins and snRNA. The instrument pressure was varied by partial closure of rota...
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| Format: | Conference item |
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2002
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| _version_ | 1826277851136000000 |
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| author | Hernández, H Krummel, D Nagai, K Robinson, C |
| author_facet | Hernández, H Krummel, D Nagai, K Robinson, C |
| author_sort | Hernández, H |
| collection | OXFORD |
| description | The non-covalent interactions which maintain protein-RNA complexes such as U1 snRNP in human spliceosome were investigated using nanoflow ESI-MS technique. The reconstituted U1 snRNP complex comprised core domain of Sm proteins and snRNA. The instrument pressure was varied by partial closure of rotary pump isolation valve and combination of cone, extractor and collision cell voltages were used to control extent of dissociation. The results show that when present in complex under similar instrumental conditions, proteins were lost individually and not as trimer or dimer. |
| first_indexed | 2024-03-06T23:35:07Z |
| format | Conference item |
| id | oxford-uuid:6d655ca9-9d00-4efc-abfb-9708d03fad2b |
| institution | University of Oxford |
| last_indexed | 2024-03-06T23:35:07Z |
| publishDate | 2002 |
| record_format | dspace |
| spelling | oxford-uuid:6d655ca9-9d00-4efc-abfb-9708d03fad2b2022-03-26T19:17:28ZDissociation of the human spliceosomal U1 snRNP complexConference itemhttp://purl.org/coar/resource_type/c_5794uuid:6d655ca9-9d00-4efc-abfb-9708d03fad2bSymplectic Elements at Oxford2002Hernández, HKrummel, DNagai, KRobinson, CThe non-covalent interactions which maintain protein-RNA complexes such as U1 snRNP in human spliceosome were investigated using nanoflow ESI-MS technique. The reconstituted U1 snRNP complex comprised core domain of Sm proteins and snRNA. The instrument pressure was varied by partial closure of rotary pump isolation valve and combination of cone, extractor and collision cell voltages were used to control extent of dissociation. The results show that when present in complex under similar instrumental conditions, proteins were lost individually and not as trimer or dimer. |
| spellingShingle | Hernández, H Krummel, D Nagai, K Robinson, C Dissociation of the human spliceosomal U1 snRNP complex |
| title | Dissociation of the human spliceosomal U1 snRNP complex |
| title_full | Dissociation of the human spliceosomal U1 snRNP complex |
| title_fullStr | Dissociation of the human spliceosomal U1 snRNP complex |
| title_full_unstemmed | Dissociation of the human spliceosomal U1 snRNP complex |
| title_short | Dissociation of the human spliceosomal U1 snRNP complex |
| title_sort | dissociation of the human spliceosomal u1 snrnp complex |
| work_keys_str_mv | AT hernandezh dissociationofthehumanspliceosomalu1snrnpcomplex AT krummeld dissociationofthehumanspliceosomalu1snrnpcomplex AT nagaik dissociationofthehumanspliceosomalu1snrnpcomplex AT robinsonc dissociationofthehumanspliceosomalu1snrnpcomplex |