Structural and Thermodynamic Studies of Synuclein Proteins Related to Parkinson’s Disease: - Metallic Systems: A Quantum Chemist's Perspective - page 54

(a) A B C D E F

(b) A B C D E F

FIGURE 2.3 (a).Structures.of.the.wild-type.α-synuclein.protein.in.aqueous.solution.(A).
obtained.from.classical.MD.simulations.at.(B).0.ns,.(C).1.ns,.(D).2.ns,.(E).3.ns,.(F).and.4.ns..
(b).( See color insert. ).Secondary.structures.of.the.wild-type.α-synuclein.in.aqueous.solu-
tion.(A).obtained.from.classical.MD.simulations.at.(B).0.ns,.(C).1.ns,.(D).2.ns,.(E).3.ns,.and.
(F).4.ns..The.α-helix.(purple),.3 10 .helix.(orange),.bridge.β.(blue),.turn.(green),.and.coil.(red).
are.depicted.

α-helix.of.the.protein.also.occur.throughout.the.course.of.the.simulation..However,.
the.C-terminal.tail.appears.to.be.the.most.lexible.part.of.the.protein..Unlike.the.gas.
phase. structure,. in. the. solvated. structure,. the. interaction. between. the. N-terminus.
and.C-terminal.side.α-helix.does.not.occur.and.we.conclude.that.this.interaction.is.
inhibited.by.the.presence.of.water.molecules.
As.with.the.solvated.wild-type.simulations,.the.structural.changes.of.the.A53T.
mutant. in. aqueous. solution. resemble. the. initial. experimental. structure. more. than.
the. equilibrated. gas-phase. structure.. By. comparing. Figure. 2.4a. through. Figure.
2.2a,. the. differences. are. evident.. The. differences. between. the. gas-phase. and.