Time-resolved laser spectroscopy with high (<100 fs) resolution is now a standard tool for studies of ultrafast processes in molecules, proteins, solid state materials and other systems. It is able to follow the key dynamical processes, such as energy and electron transfer, isomerization, bond breaking and formation and many others. Current state-of-art laser systems are able to deliver ultrashort pulses with time duration less than 20 fs in a broad spectral range extending from X-rays to mid-IR. Typically, in the transient absorption mode, which is probably the most common type of time-resolved experiment, the process of interest is initiated by exciting the sample by an excitation (pump) pulse that is, after a precise delay time, followed by a probe (typically broadband) pulse that monitors the changes in the sample caused by the excitation pulse. Here we will show a few examples how the time-resolved laser spectroscopy can be used to determine not only the function of proteins, but also how the recent advances of this technique, which includes time-resolved Raman spectroscopy or time-resolved X-ray diffraction, can relate structure and function of proteins.