WFRF:(Björling Alexander)
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 02443nam a2200289 4500 | |
| 001 | oai:gup.ub.gu.se/229793 | |
| 003 | SwePub | |
| 008 | 240528s2015 | |||||||||||000 ||eng| | |
| 020 | a 9789162896515 | |
| 024 | 7 | a 2077/406492 hdl |
| 024 | 7 | a https://gup.ub.gu.se/publication/2297932 URI |
| 040 | a (SwePub)gu | |
| 041 | a eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a vet2 swepub-contenttype |
| 072 | 7 | a dok2 swepub-publicationtype |
| 100 | 1 | a Björling, Alexander,d 1983u Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology4 aut0 (Swepub:gu)xbjale |
| 245 | 1 0 | a Detecting and Identifying Solution-structural Change in Photoactive Proteins |
| 264 | 1 | c 2015 |
| 520 | a Conformational dynamics allow proteins to fulfil their biological roles, yet the understanding of these molecular machines is largely limited to structural snapshots. Time-resolved X-ray scattering provides a possible way of uncovering such dynamics, but hinges on the ability to trigger reactions, and most critically on the ability to interpret the resulting data. This thesis explores how such experiments can be carried out and analysed. First, a computational tool for the interpretation of time-resolved X-ray scattering data is presented and tested. It is found that the method works for systems which undergo concerted domain movements, but fails for those where the structure changes in more subtle ways. The method is a potential starting point for systematic, molecular dynamics based interpretation schemes, and provides the most general and unbiased scheme yet. Further, the time-resolved X-ray scattering technique is applied to the phytochrome family of light-sensing proteins. The results establish a comprehensive mechanism of signal transduction in a particular member of the family. A comparative study shows that this mechanism is also found in several other protein relatives, implying that a core structural apparatus has been conserved and reused for various purposes during evolution. | |
| 650 | 7 | a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng |
| 653 | a Protein dynamics | |
| 653 | a X-ray scattering | |
| 653 | a Light sensing proteins | |
| 710 | 2 | a Göteborgs universitetb Institutionen för kemi och molekylärbiologi4 org |
| 856 | 4 8 | u https://gup.ub.gu.se/publication/229793 |
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