The B1 domain of protein G has been a classic model system of folding for decades, with numerous experimental and computational studies. Most of the experimental work has concluded that the protein is a two-state folder, but the evidence is mostly limited to relatively slow kinetic observations with a few structural probes and folding from a chemically denatured state. I will discuss two types of experiments that disprove the two-state model, ultrarapid mixing on the microsecond time scale with multiple probes, and observations with single molecule force spectroscopy. These results show multiple kinetic phases with different probes and very different kinetics with force compared to chemical denaturant. The overall picture is a multidimensional landscape with many pathways between folded and unfolded conformations.