We have used the method of Trp/Cys contact quenching to measure the rate of contact formation in polyglutamine and find it to be a very stiff peptide. Separation of observed rates into reaction-limited and diffusion-limited rates show that the reaction-limited rates increase (rather than decrease) slightly with length between 4 and 16 amino acids. Using Szabo, Schulten, and Schulten theory, we have modeled the results with a wormlike chain with excluded volume and find the persistence length to be about 13.0 angstrom, much longer than has been observed for other random peptides and unfolded proteins. The preferred extended conformation of polyglutamine could account for a propensity for expanded glutamine stretches to unfold the Huntington's protein and the high propensity to aggregate from a disordered monomer.