Trehalose and glycerol are low molecular mass sugars/polyols that have found widespread use in the protection of native protein states, in both short- and long-term storage of biological materials, and as a means of understanding protein dynamics. These myriad uses are often attributed to their ability to form an amorphous glassy matrix. In glycerol, the glass is formed only at cryogenic temperatures, while in trehalose, the glass is formed at room temperature, but only upon dehydration of the sample. While much work has been carried out to elucidate a mechanistic view of how each of these matrices interact with proteins to provide stability, rarely have the effects of these two independent systems been directly compared to each other. This review aims to compile decades of research on how different glassy matrices affect two types of photosynthetic proteins: (i) the Type II bacterial reaction center from Rhodobacter sphaeroides and (ii) the Type I Photosystem I reaction center from cyanobacteria. By comparing aggregate data on electron transfer, protein structure, and protein dynamics, it appears that the effects of these two distinct matrices are remarkably similar. Both seem to cause a “tightening” of the solvation shell when in a glassy state, resulting in severely restricted conformational mobility of the protein and associated water molecules. Thus, trehalose appears to be able to mimic, at room temperature, nearly all of the effects on protein dynamics observed in low temperature glycerol glasses.

海藻糖和甘油是低分子量的糖/多元醇，已广泛用于天然蛋白质状态的保护，短期和长期生物材料的存储以及作为了解蛋白质动力学的一种手段。这些无数用途通常归因于它们形成非晶态玻璃状基质的能力。在甘油中，玻璃仅在低温下形成，而在海藻糖中，玻璃在室温下形成，但仅在样品脱水时形成。尽管已经进行了大量工作来阐明每种基质如何与蛋白质相互作用以提供稳定性的机制观点，但很少将这两个独立系统的作用相互直接进行比较。球形红细菌和（ii）来自蓝细菌的I型光系统I反应中心。通过比较有关电子转移，蛋白质结构和蛋白质动力学的汇总数据，看来这两种不同基质的作用非常相似。当它们处于玻璃态时，两者似乎都导致溶剂化壳的“变紧”，从而导致蛋白质和相关水分子的构象迁移受到严格限制。因此，海藻糖似乎能够在室温下模仿在低温甘油玻璃中观察到的几乎所有对蛋白质动力学的影响。