Binding of Cu(II) ions to peptides studied by fluorescence spectroscopy and isothermal titration calorimetry.
Gdańsk, Poland. In Spectrochim Acta A Mol Biomol Spectrosc, Feb 2016
Two of them were taken from the N-terminal part of the FBP28 protein (formin binding protein) WW domain: Tyr-Lys-Thr-Ala-Asp-Gly-Lys-Thr-Tyr-NH2 (D9) and its mutant Tyr-Lys-Thr-Ala-Asn-Gly-Lys-Thr-Tyr-NH2 (D9_M) as well as two mutated peptides from the B3 domain of the immunoglobulin binding protein G derived from Streptococcus: Asp-Val-Ala-Thr-Tyr-Thr-NH2 (J1) and Glu-Val-Ala-Thr-Tyr-Thr-NH2 (J2).
Preventing fibril formation of a protein by selective mutation.
Barcelona, Spain. In Proc Natl Acad Sci U S A, Dec 2015
The origins of formation of an intermediate state involved in amyloid formation and ways to prevent it are illustrated with the example of the Formin binding protein 28 (FBP28) WW domain, which folds with biphasic kinetics.
Local vs global motions in protein folding.
Ithaca, United States. In J Chem Theory Comput, 2013
This question is addressed by analyzing folding and non-folding trajectories of a protein; as an example, the analysis is applied to the 37-residue triple β-strand WW domain from the Formin binding protein 28 (FBP28) (PDB ID: 1E0L).
Force Field Effects on a β-Sheet Protein Domain Structure in Thermal Unfolding Simulations.
Heidelberg, Germany. In J Chem Theory Comput, 2006
Motivated by thermal unfolding simulations of several WW domains, which have a three-stranded β-sheet structure, we chose the FBP28 WW domain as a well-characterized system to investigate several AMBER force fields as well as parametrization of the NPSA (Neutralized, Polarized ionizable side chains with a solvent-accessible Surface Area-dependent term) implicit solvent model.