The Trichoderma reesei cellobiohydrolase I (Cel7A) is an industrially-relevant, processive cellulase composed of a carbohydrate-binding module and a large catalytic domain connected by an O-glycosylated linker peptide of approximately 36 amino acids.  Understanding the overall mechanism by which Cel7A is able to decrystallize recalcitrant cellulose and hydrolyze cellodextrins to cellobiose should permit us to determine the rate-limiting steps in the conversion of cellulose by this enzyme.  This accomplishment will allow application of rational design strategies to the task of improving cellulase enzyme cocktails for industrial use.  Using a bottom-up approach, we apply a suite of experimental and computational techniques to understand the function of each Cel7A sub-domain.  In this study, we apply fluorescence resonance energy transfer [FRET] and molecular dynamics [MD] techniques to study the effects of glycosylation on the flexibility and conformations of the O-glycosylated Cel7A linker domain.  The resulting conformational states that the linker peptide adopts provide clues to the roles that linker flexibility may play in the processivity of the Cel7A enzyme.