Li H, Carrion-Vazquez M, Oberhauser A F, Marszalek P E, Fernandez J M
Department of Physiology and Biophysics, Mayo Foundation, Rochester, Minnesota 55905, USA.
Nat Struct Biol. 2000 Dec;7(12):1117-20. doi: 10.1038/81964.
Immunoglobulin-like modules are common components of proteins that play mechanical roles in cells such as muscle elasticity and cell adhesion. Mutations in these proteins may affect their mechanical stability and thus may compromise their function. Using single molecule atomic force microscopy (AFM) and protein engineering, we demonstrate that point mutations in two beta-strands of an immunoglobulin module in human cardiac titin alter the mechanical stability of the protein, resulting in mechanical phenotypes. Our results demonstrate a previously unrecognized class of phenotypes that may be common in cell adhesion and muscle proteins.
免疫球蛋白样模块是蛋白质的常见组成部分，在细胞中发挥机械作用，如肌肉弹性和细胞黏附。这些蛋白质中的突变可能会影响其机械稳定性，进而可能损害其功能。通过单分子原子力显微镜（AFM）和蛋白质工程技术，我们证明人类心脏肌联蛋白中免疫球蛋白模块的两条β链上的点突变会改变蛋白质的机械稳定性，从而产生机械表型。我们的结果证明了一类以前未被认识到的表型，这类表型可能在细胞黏附蛋白和肌肉蛋白中很常见。
