Practical Global Optimization Computing Methods in Molecular Modelling

Lieferzeit: Lieferbar innerhalb 14 Tagen

68,00 

for Atomic-resolution Structures of Amyloid Fibrils

ISBN: 3846521396
ISBN 13: 9783846521397
Autor: Zhang, Jiapu
Verlag: LAP LAMBERT Academic Publishing
Umfang: 196 S.
Erscheinungsdatum: 14.10.2011
Auflage: 1/2011
Format: 1.2 x 22 x 15
Gewicht: 310 g
Produktform: Kartoniert
Einband: KT
Artikelnummer: 1299021 Kategorie:

Beschreibung

Due to the unstable, noncrystalline and insoluble nature of some proteins, the technologies such as X-ray crystallography, NMR (nuclear magnetic resonance) spectroscopy and dual polarization interferometry etc sometimes cannot produce the 3D structures of these proteins. In this condition, molecular modeling (MM) might have been the only strategy to get the 3D structures. The non-covalent interactions such as hydrogen bonding (HB), ionic interactions (SB), Van Der Waals forces (VDW), and hydrophobic packing (HP) are driving the proteins to be able to perform their biological functions. The author has found some SBs play a key role in prion diseases revealed from rabbit prion protein. Neurodegenerative diseases are amyloid fibril diseases. This book studies the HB, VDW, HP interactions for MM of amyloid fibrils in global optimization (GO). The GO MM-algorithms of this book should be very useful in materials science, drug design, IT, operations research, biostatistics and bioinformatics etc research fields. This book was written without advanced mathematical formulas thus it is easily readable for people in wide areas of sciences, engineering, IT, medicine, physiology, education,etc

Autorenporträt

This book (dedicated to his father) was written based on Dr Jiapu Zhang's PhD thesis. Dr Jiapu Zhang was born in 1971 in Fei County, Shandong, P.R.China. He got his bachelor degree in 1993 and 1st masters degree in research in 1996 from China, 2nd masters degree in research in 2000 from National University of Singapore, and 1st postdoc from CSIRO.

Das könnte Ihnen auch gefallen …