Elastin-like polypeptides (ELPs) are biocompatible polymers exhibiting lower critical solution temperature (LCST) behavior, making them valuable in various applications, including drug delivery and tissue engineering. This study addresses the atomistic-level understanding of ELP self-assembly, focusing on their internal structural dynamics. Conventional proton-detected nuclear magnetic resonance (NMR) spectroscopy faces limitations in studying ELP aggregates due to accelerated proton exchange processes, which cause significant resonance broadening. Herein, we show how to overcome this hurdle by using carbon-13-detected NMR. This method mitigates issues related to amide proton exchange, allowing for a residue-resolved view of the internal configuration of ELP aggregates. With this method, we record residue-resolved