Davies, HA, Phelan, MM and Madine, J 
ORCID: 0000-0001-9963-5871
(2016)
<SUP>1</SUP>H, <SUP>15</SUP>N and <SUP>13</SUP>C assignment of the amyloidogenic protein medin using fast-pulsing NMR techniques.
BIOMOLECULAR NMR ASSIGNMENTS, 10 (1).
pp. 75-77.
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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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Medin, Amyloid, Fast-pulsing NMR, Resonance assignment, Cardiovascular, Fibril |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 13 Jan 2016 14:44 |
| Last Modified: | 05 Oct 2023 11:25 |
| DOI: | 10.1007/s12104-015-9641-z |
| Publisher's Statement : | © The Author(s) 2015.This article is published with open access at Springerlink.com . This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creative commons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/2046361 |
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