An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.
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AFM Imaging Reveals Topographic Diversity of Wild Type and Z Variant Polymers of Human α1-Proteinase InhibitorStructural and functional adaptation of Haloferax volcanii TFEα/β.α1-Antitrypsin deficiency.Ion mobility coupled to native mass spectrometry as a relevant tool to investigate extremely small ligand-induced conformational changes.
P2860
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.
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2015 nî lūn-bûn
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name
An integrative approach combin ...... titrypsin upon ligand binding.
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type
label
An integrative approach combin ...... titrypsin upon ligand binding.
@en
prefLabel
An integrative approach combin ...... titrypsin upon ligand binding.
@en
P2093
P2860
P50
P356
P1433
P1476
An integrative approach combin ...... titrypsin upon ligand binding.
@en
P2093
David A Lomas
Ganesh N Sivalingam
Geraldine Levy
John Christodoulou
John Kirkpatrick
Konstantinos Thalassinos
Mun Peak Nyon
Tanya Prentice
P2860
P304
P356
10.1002/PRO.2706
P577
2015-07-14T00:00:00Z