AI Article Synopsis
- A new photo-crosslinking/mass spectrometry method is introduced to study the structure of folded proteins.
- This technique uses a reactive photo-leucine to stabilize specific regions in β-turn and β-hairpin domains of proteins.
- It enables researchers to gain insights into the native 3D structure of proteins by examining these clamped regions.
Article Abstract
From folded to crosslinked proteins. A new promising photo-crosslinking/mass spectrometry method for the structural characterisation of folded proteins is highlighted. A reactive photo-leucine can clamp the front residues in β-turn and β-hairpin domains, thus allowing us to look into the specific native 3D structure of proteins.
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| http://dx.doi.org/10.1002/cbic.201200742 | DOI Listing |
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