NDLI: $^{1}$H, $^{15}$N and $^{13}$C assignment of the amyloidogenic protein medin using fast-pulsing NMR techniques

Content Provider	Springer Nature Link
Author	Davies, H. A. Phelan, M. M. Madine, J.
Copyright Year	2015
Abstract	Thirty-one proteins are known to form extracellular fibrillar amyloid in humans. Molecular information about many of these proteins in their monomeric, intermediate or fibrillar form and how they aggregate and interact to form the insoluble fibrils is sparse. This is because amyloid proteins are notoriously difficult to study in their soluble forms, due to their inherent propensity to aggregate. Using recent developments in fast NMR techniques, band-selective excitation short transient and band-selective optimized flip-angle short-transient heteronuclear multiple quantum coherence we have been able to assign a 5 kDa full-length amyloidogenic protein called medin. Medin is the key protein component of the most common form of localised amyloid with a proposed role in aortic aneurysm and dissection. This assignment will now enable the study of the early interactions that could influence initiation and progression of medin aggregation. The chemical shifts have been deposited in the BioMagRes-Bank accession Nos. 25399 and 26576.
Starting Page	75
Ending Page	77
Page Count	3
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	10
Issue Number	1
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2015-09-16
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Medin Amyloid Fast-pulsing NMR Resonance assignment Cardiovascular Fibril Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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1H, 15N and 13C assignment of the amyloidogenic protein medin using fast-pulsing NMR techniques

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