PXD015044

PXD015044 is an original dataset announced via ProteomeXchange.

Title	Insight into the structure of the “unstructured” tau protein
Description	Here, we apply a recently-developed approach for de novo protein structure determination based on the incorporation of short-distance crosslinking data as constraints in discrete molecular dynamics simulations (CL-DMD), for the determination of the conformational ensemble of tau protein in solution. The predicted structure may facilitate an understanding of the misfolding and oligomerization pathways of the tau protein.
HostingRepository	PRIDE
AnnounceDate	2019-10-08
AnnouncementXML	Submission_2019-10-21_00:04:28.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Karl Makepeace
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2019-08-16 01:09:46	ID requested
1	2019-10-08 00:09:05	announced
⏵ 2	2019-10-21 00:04:29	announced	2019-10-21: Updated publication reference for PubMed record(s): 26789759.

Chin AF, Toptygin D, Elam WA, Schrank TP, Hilser VJ, Phosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein. Biophys J, 110(2):362-371(2016) [pubmed]

submitter keyword: cross-linking, tau, intrinsically disordered proteins, IDP, discrete molecular dynamics, CL-DMD

Christoph H. Borchers
contact affiliation	1. University of Victoria Genome BC Proteomics Centre, University of Victoria, Victoria, British Columbia, Canada 2. Segal Cancer Proteomics Centre, Lady Davis Institute, Jewish General Hospital, McGill University, Montreal, Quebec, Canada 3. Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada 4. Gerald Bronfman Department of Oncology, Jewish General Hospital, Montreal, Quebec, Canada
contact email	christoph.borchers@mcgill.ca
lab head
Karl Makepeace
contact affiliation	University of Victoria
contact email	karlm@uvic.ca
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/10/PXD015044

PRIDE project URI

• PRIDE
  1. PXD015044
     1. Label: PRIDE project
     2. Name: Insight into the structure of the “unstructured” tau protein