Andere Kunden interessierten sich auch für
![Quantum Simulations of Materials and Biological Systems]( "Quantum Simulations of Materials and Biological Systems")
Quantum Simulations of Materials and Biological Systems74,99 €![Plant Heat shock protein]( "Plant Heat shock protein")
Plant Heat shock protein32,99 €![Cholesterol Transporters of the START Domain Protein Family in Health and Disease]( "Cholesterol Transporters of the START Domain Protein Family in Health and Disease")
Cholesterol Transporters of the START Domain Protein Family in Health and Disease74,99 €![Molecular Mechanisms Controlling Transmembrane Transport]( "Molecular Mechanisms Controlling Transmembrane Transport")
Molecular Mechanisms Controlling Transmembrane Transport147,99 €![Cholesterol Transporters of the START Domain Protein Family in Health and Disease]( "Cholesterol Transporters of the START Domain Protein Family in Health and Disease")
Cholesterol Transporters of the START Domain Protein Family in Health and Disease74,99 €![I Domain Integrins]( "I Domain Integrins")
I Domain Integrins74,99 €![Functional characterization of lipid binding of P122 START domain]( "Functional characterization of lipid binding of P122 START domain")
Functional characterization of lipid binding of P122 START domain26,99 €
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.