The hydrophobic core in Bcl-xL composed of Trp137, Ile140, Trp181, Ile182, Trp188 and Phe191 is highly conserved and essential for protein folding, protein stability and binding affinity with BH3-peptide. 9 mutants of Ile140 residue were constructed and characterized in order to get
better understanding of the effect of the hydrophobic core. Binding assay demonstrated that binding affinities between 4 charged mutants and BH3-peptide were significantly weakened or lost, suggesting that the integrity of the hydrophobic core has close relationship with binding. The CD spectroscopy
results indicated that disruption of the hydrophobic core may affect local conformation within the protein and result in intrinsic inactivity. Further chemical-induced protein folding results on these 4 mutants revealed that the conserved hydrophobic core is also important for the protein
Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.