acterize dynamics of such systems are expected to benefit many fields where IDPs and peptide aggregates with lipids or other biomolecules are relevant, ranging from design of drugs targeting disordered proteins and novel materials based on silk proteins to disordered peptides with potential antimicrobial activity and nanodiscs with biomedical relevance . Here we present a rapid way of determining average rotational timescales of residues in folded and disordered proteins, as well as in peptides in micelles, using data that can be routinely measured experimentally and is widely available in the literature.