Data from: Formation of beta-strands in the extramembrane controls dimerization of transmembrane helices in amyloid precursor protein C99 intrinsically disordered domains
Published: 18 July 2022| Version 1 | DOI: 10.17632/j6rtdskrvc.1
Contributors:
, , , , , , Description
Within this data set are 1) Conformations of the 99-residue C-terminal domain of Amyloid Precursor Protein (C99), which is processed to form amyloid beta, in a POPC lipid bilayer and 150 mM NaCl aqueous solvent. 2) Input parameters for gREST simulations of C99 monomer and homodimer in the GENESIS molecular dynamics simulation package. 3) NMR peak intensity ratios (I/I0) due to addition of paramagnetic probes measured at dilute C99 concentrations.
Files
Institutions
National Institutes of Health, Boston University, University of Texas at Austin, Vanderbilt University, RIKEN Global Research Cluster
Categories
Membrane Protein, Molecular Dynamics, Intrinsically Disordered Protein, Amyloid Precursor Protein