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Protein Folding An Introduction

:	Cláudio M. Gomes, Patrícia F.N. Faísca
:	Protein Folding An Introduction
:	Springer-Verlag
:	9783319008820
:	1
:	CHF 48.00
:

:	Mikrobiologie
:	English

:	74
:	Wasserzeichen/DRM
:	PC/MAC/eReader/Tablet
:	PDF

This snapshot volume is designed to provide a smooth entry into the field of protein folding. Presented in a concise manner, each section introduces key concepts while providing a brief overview of the relevant literature. Outlook subsections will pinpoint specific aspects related to emerging methodologies, concepts and trends.

Cláudio M. Gomes is Associate Professor of Biochemistry at the Department of Chemistry and Biochemistry of the Faculty of Sciences (DQB-FCUL), University of Lisbon, where he heads the 'Protein Folding and Misfolding Laboratory' within BioISI - Biosystems and Integrative Sciences Institute. He is a Gulbenkian Ph.D. program in Biology and Medicine alumni, and he has obtained is PhD (1999) and Habilitation (2013) in Biochemistry at Universidade Nova de Lisboa. He is an expert on structural biology, biochemistry and biophysics of protein stability, folding and misfolding, with +110 articles published (h-index 26). His current interests focus on mechanisms of protein aggregation in the context of complex biomedical problems such as those arising in Alzheimer's neurodegeneration.

Patrícia F.N. Faísca is Assistant Professor of Physics at the Physics Department of the Faculty of Sciences (DF-FCUL), University of Lisbon, and principal investigator at BioISI - Biosystems and Integrative Sciences Institute. She received her PhD (Physics) in 2002 at the University of Warwick (UK), as part of the Gulbenkian PhD Program in Biology and Medicine. She has a broad interdisciplinary education covering Physics, Biology and Mathematics. Her research on computational biophysics is based on the use of molecular simulations, especially of coarse-grained models. Her current research interests focus on the folding of knotted proteins, and on protein misfolding and aggregation in a disease-related context.

	Preface	7
	Contents	9
	About the Authors	11
	1 Protein Folding: An Introduction	12
	1 Protein Structure—How Is Structure Maintained?	12
	1.1 The Dawn of Protein Structural Biology	12
	1.2 The Universe of Protein Structures	13
	1.3 Physical Interactions Stabilising Proteins	18
	1.4 Protein Dynamics and Solvation	20
	2 Protein Folding—Why Is Structure Acquired?	21
	2.1 The Anfinsen Experiments	22
	2.2 The Thermodynamic Hypothesis	24
	2.3 Driving Forces for Protein Folding—Hydrophobic Effect and the Thermodynamics of Protein Folding	25
	3 Folding Kinetics and Mechanisms: How Is Structure Acquired?	31
	3.1 Two-State Cooperativity in Protein Folding	31
	3.2 The Levinthal Paradox and the Timescale of Protein Folding	37
	3.3 Mechanisms of Protein Folding	38
	3.4 The Nucleation Condensation Mechanism of Protein Folding	39
	3.5 Phi-value Analysis and the Structure of the Folding Transition State	39
	3.6 The Energy Landscape and Folding Funnels	40
	3.7 The Importance of Native Geometry as a Determinant of Folding Rates	42
	3.8 The Folding Mechanism of Knotted Proteins	43
	4 Protein Misfolding: Why Proteins Misbehave?	45
	4.1 Protein Folding In Vivo	45
	4.2 Protein Misfolding and Aggregation	49
	4.3 Protein Misfolding Diseases	51
	4.4 The Amyloid State	52
	4.5 Mechanism and Kinetics of Protein Aggregation	56
	4.6 Aggregation Propensity	60
	5 Methods for Protein Folding	61
	5.1 Biophysical Spectroscopies	61
	5.2 Computational Methods	64
	References	65