We present design of novel low-power homonuclear dipolar recoupling experiments for magic-angle-spinning solid-state NMR studies of proteins. The pulse sequences are developed by combining principles of symmetry-based dipolar recoupling and optimal control-based pulse sequence design. The scaffold of the pulse sequences is formed by known CN-type recoupling sequences, while the intrinsic sequence elements are designed using optimal control. This procedure allows for the development of high-performance pulse sequences demanding significantly weaker rf fields than previous symmetry-based pulse sequences while compensating for rf inhomogeneity and providing excitation over relevant ranges of chemical shifts for biological applications. The new recoupling experiments, referred to as optimal control CN ((OC)CN), are demonstrated numerically and experimentally by two-dimensional (2D) (13)C-(13)C and three-dimensional (3D) (15)N-(13)C-(13)C chemical shift correlation experiments on uniformly (13)C, (15)N-labeled ubiquitin. Exploiting the double-quantum, band-selective dipolar recoupling properties of the (OC)CN experiments, we demonstrate significant sensitivity enhancement for 2D and 3D correlation spectra showing exclusively one- or two-bond correlations.