Molecular Dynamics Simulations of the Neu Transmembrane Domain
Physical Characterization of Native and Mutated Neu in a Membrane Environment
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Neu is a membrane-bound protein whose structureincludes a single helix which spans the width of acellular membrane. It is a growth factor receptorwhich dimerizes (forms pairs) when signaling cellgrowth and proliferation. Key mutations at a specificlocation in the transmembrane domain (TMD) of the neuprotein have been demonstrated to result in permanentdimerization of mutated pairs, and are simultaneouslyassociated with the formation of cancerous tumors.The physical effects of these key point mutationsthat lead to such permanent dimerization are notknown. Atomistic molecular dynamics (MD) simul...
Neu is a membrane-bound protein whose structure
includes a single helix which spans the width of a
cellular membrane. It is a growth factor receptor
which dimerizes (forms pairs) when signaling cell
growth and proliferation. Key mutations at a specific
location in the transmembrane domain (TMD) of the neu
protein have been demonstrated to result in permanent
dimerization of mutated pairs, and are simultaneously
associated with the formation of cancerous tumors.
The physical effects of these key point mutations
that lead to such permanent dimerization are not
known. Atomistic molecular dynamics (MD) simulations,
whereby Newton's equations of motion are numerically
solved for the atoms in the neu TMD and its
surrounding membrane environment, provide further
physical insight into this important problem. This
book reviews the MD simulation method as well as
previous work characterizing the neu protein; the
book further examines the results of detailed MD
simulations of native and mutant neu TMDs in hydrated
membrane environments. The reader should have some
basic background in biophysical chemistry, Newtonian
dynamics, and statistical mechanics.
includes a single helix which spans the width of a
cellular membrane. It is a growth factor receptor
which dimerizes (forms pairs) when signaling cell
growth and proliferation. Key mutations at a specific
location in the transmembrane domain (TMD) of the neu
protein have been demonstrated to result in permanent
dimerization of mutated pairs, and are simultaneously
associated with the formation of cancerous tumors.
The physical effects of these key point mutations
that lead to such permanent dimerization are not
known. Atomistic molecular dynamics (MD) simulations,
whereby Newton's equations of motion are numerically
solved for the atoms in the neu TMD and its
surrounding membrane environment, provide further
physical insight into this important problem. This
book reviews the MD simulation method as well as
previous work characterizing the neu protein; the
book further examines the results of detailed MD
simulations of native and mutant neu TMDs in hydrated
membrane environments. The reader should have some
basic background in biophysical chemistry, Newtonian
dynamics, and statistical mechanics.
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