We propose to perform stopped-flow time-resolved small-angle x-ray scattering studies of the refolding of sperm whale apomyoglobin under the same conditions used in a recent folding study employing stopped-flow circular dichroism and pulse labeling NMR techniques. We want to obtain further information regarding the size and time-scale of formation of a kinetic molten globule intermediate on the apolmyoglobin refolding pathway. The insights provided by these experiments will help to further interpret the NMR results, and should lead to a clearer understanding of the folding mechanism of apomyoglobin in particular and of proteins in general.