During the past decades, NMR spectroscopy has emerged as a unique tool for the study of protein dynamics. Indeed, relaxation studies on isotopically labeled proteins can provide information on the overall motions as well as the internal fast, sub-nanosecond, dynamics. Therefore, the interpretation and the prediction of spin relaxation rates in proteins are important issues that have motivated numerous theoretical and methodological developments, including the description of overall dynamics and its possible coupling to internal mobility, the introduction of models of internal dynamics, the determination of correlation functions from experimental data, and the relationship between relaxation and thermodynamical quantities. A brief account of recent developments that have proven useful in this domain are presented.