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.
Interaction between Common Genetic Variants and Total Fat Intake on Low-Density Lipoprotein Peak Particle Diameter: A Genome-Wide Association Study.
Québec, Canada. In J Nutrigenet Nutrigenomics, 2014
RESULTS: The GWAS analyses 29 identified independent SNP × total fat intake interaction effects on the LDL-PPD at p < 10(-5), including SNPs in the following genes: ABCG2, CPA3, FNBP1, KCNQ3, NBAS, NCALD, OPRL1, NKAIN2, SH3BGRL2, SOX5, and SUSD4.
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).
Relation between free energy landscapes of proteins and dynamics.
Ithaca, United States. In J Chem Theory Comput, 2010
By examining the molecular dynamics (MD) of protein folding trajectories, generated with the coarse-grained UNRES force field, for the B-domain of staphylococcal protein A and the triple β-strand WW domain from the Formin binding protein 28 (FBP), by principal component analysis (PCA), it is demonstrated how different free energy landscapes (FELs) and folding pathways of trajectories can be, even though they appear to be very similar by visual inspection of the time-dependence of the root-mean-square deviation (rmsd).