Nathan Ira Nicely

author keywords: caspase recruitment domain; protein folding; folding kinetics; parallel folding channels; sequential mixing stopped-flow

MeSH headings : Apoptotic Protease-Activating Factor 1 / chemistry; Apoptotic Protease-Activating Factor 1 / metabolism; Crystallography, X-Ray; Fluorescence; Kinetics; Models, Biological; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Thermodynamics

TL;DR: Examination of the equilibrium and kinetic folding of the CARD of Apaf-1 (apoptotic protease activating factor 1), which consists of 97 amino acid residues, at pH 6 and pH 8 showed that the native ensemble is formed rapidly upon refolding, in contrast to other CARDs in which folding appears to be dominated by formation of kinetic traps. (via Semantic Scholar)

MeSH headings : Amino Acid Sequence; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Guanosine Diphosphate / chemistry; Guanosine Diphosphate / metabolism; Guanosine Triphosphate / analogs & derivatives; Guanosine Triphosphate / chemistry; Guanosine Triphosphate / metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; rap GTP-Binding Proteins / chemistry; rap GTP-Binding Proteins / metabolism; ras Proteins / chemistry; ras Proteins / metabolism

TL;DR: Clustering of conserved residues on the surface of Ral-GppNHp identifies two putative sites for protein-protein interaction, one of which is adjacent to switch I and the other is modulated by switch II and is obstructed in RAl-GDP. (via Semantic Scholar)