New insights into the protein stabilizing effects of trehalose by comparing with sucrose
Kajsa Ahlgren, Christoffer Olsson, Inna Ermilova, Jan Swenson
Abstract
trehalose forms less hydrogen bonds to the protein surface than sucrose. Furthermore, the rotational motion around dihedrals between the two glucose rings of trehalose is slower than in the case of the dihedrals between the glucose and fructose rings of sucrose. This leads to a less perturbed protein structure in the case of trehalose. The observations indicate that an aqueous environment closest to the protein molecules is beneficial for an efficient bioprotective solution.
Topics & Concepts
TrehaloseAqueous solutionChemistrySucroseCrystallographyMyoglobinNeutron scatteringMolecular dynamicsSugarHydrogen bondFructoseNeutron diffractionMoleculeProtein dynamicsBiophysicsChemical physicsNeutronBiochemistryComputational chemistryPhysical chemistryOrganic chemistryCrystal structureBiologyPhysicsQuantum mechanicsEnzyme Structure and FunctionHemoglobin structure and functionProtein Structure and Dynamics