Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
Lysozyme from lambda bacteriophage (lambda lysozyme) is an 18 kDa globular protein displaying some of the structural features common to all lysozymes; in particular, lambda lysozyme consists of two structural domains connected by a helix, and has its catalytic residues located at the interface betwe...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2010
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| _version_ | 1797058295491461120 |
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| author | Di Paolo, A Duval, V Matagne, A Redfield, C |
| author_facet | Di Paolo, A Duval, V Matagne, A Redfield, C |
| author_sort | Di Paolo, A |
| collection | OXFORD |
| description | Lysozyme from lambda bacteriophage (lambda lysozyme) is an 18 kDa globular protein displaying some of the structural features common to all lysozymes; in particular, lambda lysozyme consists of two structural domains connected by a helix, and has its catalytic residues located at the interface between these two domains. An interesting feature of lambda lysozyme, when compared to the well-characterised hen egg-white lysozyme, is its lack of disulfide bridges; this makes lambda lysozyme an interesting system for studies of protein folding. A comparison of the folding properties of lambda lysozyme and hen lysozyme will provide important insights into the role that disulfide bonds play in the refolding pathway of the latter protein. Here we report the (1)H, (13)C and (15)N backbone resonance assignments for lambda lysozyme by heteronuclear multidimensional NMR spectroscopy. These assignments provide the starting point for detailed investigation of the refolding pathway using pulse-labelling hydrogen/deuterium exchange experiments monitored by NMR. |
| first_indexed | 2024-03-06T19:48:27Z |
| format | Journal article |
| id | oxford-uuid:23253517-d518-4c51-ac73-8e5df110c8eb |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:48:27Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:23253517-d518-4c51-ac73-8e5df110c8eb2022-03-26T11:42:40ZBackbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:23253517-d518-4c51-ac73-8e5df110c8ebEnglishSymplectic Elements at Oxford2010Di Paolo, ADuval, VMatagne, ARedfield, CLysozyme from lambda bacteriophage (lambda lysozyme) is an 18 kDa globular protein displaying some of the structural features common to all lysozymes; in particular, lambda lysozyme consists of two structural domains connected by a helix, and has its catalytic residues located at the interface between these two domains. An interesting feature of lambda lysozyme, when compared to the well-characterised hen egg-white lysozyme, is its lack of disulfide bridges; this makes lambda lysozyme an interesting system for studies of protein folding. A comparison of the folding properties of lambda lysozyme and hen lysozyme will provide important insights into the role that disulfide bonds play in the refolding pathway of the latter protein. Here we report the (1)H, (13)C and (15)N backbone resonance assignments for lambda lysozyme by heteronuclear multidimensional NMR spectroscopy. These assignments provide the starting point for detailed investigation of the refolding pathway using pulse-labelling hydrogen/deuterium exchange experiments monitored by NMR. |
| spellingShingle | Di Paolo, A Duval, V Matagne, A Redfield, C Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda. |
| title | Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda. |
| title_full | Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda. |
| title_fullStr | Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda. |
| title_full_unstemmed | Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda. |
| title_short | Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda. |
| title_sort | backbone 1h 13c and 15n resonance assignments for lysozyme from bacteriophage lambda |
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