The nature and rate of vibrational energy flow in proteins influence reaction kinetics, allosteric transitions, and are important in maintaining protein structure during function. We discuss calculations of rates and pathways for vibrational energy flow in a number of globular proteins. Among these calculations, we compute quantum mechanically the rate of anharmonic decay of the vibrational modes. Computed rates in the amide I region match the available lifetimes measured by pump-probe spectroscopy from 10 K to 310 K. Over this temperature range the experimental amide I lifetimes are nearly independent of temperature. We find that lifetimes of most higher frequency vibrational modes of proteins vary little with temperature, consistent with a propensity that we find for localized modes of a protein close in space to be typically separated by several hundred wave numbers. We shall also discuss the anomalous diffusion of vibrational energy in proteins, and the computation of thermal transport coefficients.