Secondary structure elements of many protein families exhibit differential conservation on their opposing faces. Amphipathic helices and beta-sheets by definition possess this property, and play crucial functional roles. This type of evolutionary trajectory of a protein family is usually critical to the functions of the protein family, as well as in creating functions within subfamilies. That is, differential conservation maintains properties of a protein structure related to its orientation, and that are important in packing, recognition, and catalysis. Here I define and formulate a new concept, called the selection moment, that detects this evolutionary process in protein sequences. A treatment of its various applications is detailed.