Chitin is the primary structural material of insect and crustacean exoskeletons and fungal and algal cell walls, and as such it is the one of the most abundant biological materials on Earth. Chitin forms linear polymers of beta 1,4-linked-N-acetyl-D-glucosamine (GlcNAc), and in Nature, enzyme cocktails deconstruct chitin to GlcNAc. The mechanism of chitin deconstruction, like that of cellulose deconstruction, has been under investigation due to its importance in the global carbon cycle and in production of renewable and sustainable products from biological matter. To further understand the nanoscale properties of chitin, here we simulate crystals of a-chitin, which is the most prevalent form in Nature. We find excellent agreement with the recently reported crystal structure and we report the salient features of the simulations related to crystalline stability. We also compute the thermodynamic work required to peel individual chains from a-chitin surfaces, which a chitinase enzyme must conduct to deconstruct chitin. Compared with previous simulations of native plant cellulose I beta, alpha-chitin exhibits higher decrystallization work for chains in the middle of surfaces and similar work for chains on the edges of crystals. Unlike cellulose, the free energy profile is dominated by a single bifurcated hydrogen bond between chains formed by the GlcNAc side chains and the O6 atoms on the primary alcohol group. This study highlights the molecular features of chitin that make it such a tough, recalcitrant material, and provides a key thermodynamic parameter in our quantitative understanding of how enzymes contribute to the turnover of carbohydrates in the biosphere.