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Molecular Dynamics Simulations of the Neu Transmembrane Domain: Physical Characterization of Native and Mutated Neu in a Membrane Environment - Couverture souple

Van Der Ende, Bryan

 
9783639127621: Molecular Dynamics Simulations of the Neu Transmembrane Domain: Physical Characterization of Native and Mutated Neu in a Membrane Environment
Couverture souple
ISBN 10 : 3639127625 ISBN 13 : 9783639127621
Editeur : VDM Verlag, 2009

Synopsis

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.

Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.

Présentation de l'éditeur

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.

Biographie de l'auteur

Dr. Bryan van der Ende studied physics in Canada: in Burnaby, British Columbia and Guelph, Ontario. He is currently a postdoctoral fellow in Utrecht, The Netherlands.

Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.

Éditeur
VDM Verlag
Date d'édition
2009
Langue
anglais
ISBN 10 
3639127625
ISBN 13 
9783639127621
Reliure
Broché
Nombre de pages
196
Coordonnées du fabricant
non disponible
Personne responsable
non disponible