Elucidating the mechanism of protein folding is an intriguing and challenging task. We have proposed a novel parameter, long-range order (LRO) for a protein from the knowledge of long-range contacts (contacts between two residues that are close in space and far in the sequence) in protein structure. A simple statistical method has been developed for predicting the folding rate of two-state proteins using LRO and we found an excellent agreement between the predicted and experimental protein folding rates. Further, we found that the conformational properties, short and medium-range energy and long-range contacts are the major determinants for transition state structures of two-state proteins.