The collapse of the polypeptide backbone is an integral part of protein folding. Using polyglycine as a probe, we explore the nonequilibrium pathways of protein collapse in water. We find that the collapse depends on the competition between hydration effects and intrapeptide interactions. Once intrapeptide van der Waal interactions dominate, the chain collapses along a nonequilibrium pathway characterized by formation of pearl-necklace-like local clusters as intermediates that eventually coagulate into a single globule. By describing this coarsening through the contact probability as a function of distance along the chain, we extract a time-dependent length scale that grows in a linear fashion. The collapse dynamics is characterized by a dynamical critical exponent z approximate to 0.5 that is much smaller than the values of z = 1-2 reported for nonbiological polymers. This difference in the exponents is explained by the instantaneous formation of intrachain hydrogen bonds and local ordering that may be correlated with the observed fast folding times of proteins.