Adsorption processes of proteins on solid surfaces have been investigated over many years but, due to their complexity, it is still difficult to predict their behavior. Indeed, proteins are highly structured polyelectrolytes, polyamphiphiles, which, in addition, are often only marginally stable. While interacting with a solid surface, they often change their structure and parallelly increase their anchoring to the surface. The influence of different parameters entering in these adsorption processes, such as the substrate charge, the substrate hydrophobicity and the protein stability, will be discussed. The dynamics of these processes will, in particular, be mentionned. It will appear that the time scales entering in adsorption processes range from tens of hours down to milliseconds. While the characteristic interaction time needed for fibrinogen, a plasma protein, to bind to a silica surface appears to be of the order of 50ms, the exchange ability of a ribonuclease molecule adsorbed on a titanium oxyde surface changes with a characteristic time of the order of 10 hours. Structural changes are observed in the adsorbed layer over similar time scales. Recent results obtained in this field, in particular by Infrared Spectroscopy and by Atomic Force Microscopy, will be presented