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Proteins|September 15, 2011
Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditionsWenli Meng, Daniel P RaleighBiochemistry|March 14, 2012
Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanolsPing Cao, Daniel P RaleighJournal of the American Chemical Society|March 6, 2010
Ester to amide switch peptides provide a simple method for preparing monomeric islet amyloid polypeptide under physiologically relevant conditions and facilitate investigations of amyloid formationPing Cao, Daniel P RaleighPlos One|September 27, 2014
General amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomersHui Wang, Daniel P RaleighJournal of Molecular Biology|May 22, 2007
Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9Satoshi Sato, Daniel P RaleighJournal of Molecular Biology|June 24, 2010
A critical assessment of putative gatekeeper interactions in the villin headpiece helical subdomainShifeng Xiao, Daniel P RaleighJournal of Molecular Biology|June 8, 2002
pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9Satoshi Sato, Daniel P RaleighJournal of Molecular Biology|January 4, 2011
Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediatesFanling Meng, Daniel P RaleighBiochemistry|March 25, 2014
The ability of insulin to inhibit the formation of amyloid by pro-islet amyloid polypeptide processing intermediates is significantly reduced in the presence of sulfated glycosaminoglycansHui Wang, Daniel P RaleighMethods in Molecular Biology (Clifton, N.J.)|October 11, 2015
In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar VesiclesPing Cao, Daniel P RaleighPageof 19