Julio M. Fernandez

TL;DR: Single-molecule atomic force microscopy was used to investigate the mechanical properties of titin, the giant sarcomeric protein of striated muscle, and refolding of immunoglobulin domains was observed.

TL;DR: It is shown that mechanical stretching of single cytoplasmic proteins can activate binding of other molecules and molecular mechanotransduction can occur by protein binding after exposure of buried binding sites in the talin-vinculin system.

TL;DR: The results indicate that mechanical unfolding of a single protein by AFM does indeed reflect the same event that is observed in traditional unfolding experiments, and the way is now open for the extensive use of AFM to measure folding reactions at the single-molecule level.

TL;DR: It is suggested that the extensibility of the modular fibronectin type III region may be important in allowing tenascin–ligand bonds to persist over long extensions, and of widespread use in extracellular proteins containing such domain.

TL;DR: This work reports the elongation of single proteins to have multiple copies of single immunoglobulin domains of human cardiac titin using the atomic force microscope, and finds an abrupt extension of each domain by ∼7 Å before the first unfolding event, likely to be an important previously unrecognized component of titin elasticity.