Donev Protein Structure and Diseases

1. Auflage 2011
ISBN: 978-0-12-381263-6
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band Volume 83, 312 Seiten, Web PDF

Reihe: Advances in Protein Chemistry and Structural Biology

Structural genomics is the systematic determination of 3D structures of proteins representative of the range of protein structure and function found in nature. The goal is to build a body of structural information that will predict the structure and potential function for almost any protein from knowledge of its coding sequence. This is essential information for understanding the functioning of the human proteome, the ensemble of tens of thousands of proteins specified by the human genome. While most structural biologists pursue structures of individual proteins or protein groups, specialists in structural genomics pursue structures of proteins on a genome wide scale. This implies large-scale cloning, expression and purification. One main advantage of this approach is economy of scale. - Examines the three dimensional structure of all proteins of a given organism, by experimental methods such as X-ray crystallography and NMR spectroscopy - Looks at structural genomics as a foundation of drug discovery as discovering new medicines is becoming more challenging and the pharmaceutical industry is looking to new technologies to help in this mission

Autoren/Hrsg.

Donev, Rossen

Inhaltsverzeichnis

1;Front Cover;1
2;Protein Structure and Diseases;4
3;Copyright;5
4;Contents;6
5;Chapter 1: Graphical representation and mathematical characterization of protein sequences and applications to viral proteins;10
5.1;I. Introduction;11
5.2;II. Graphical Methods;18
5.3;III. Application to Viral Proteins;30
5.4;IV. Conclusion;41
5.5;References;41
6;Chapter 2: Structural, thermodynamic, and mechanistical studies in uroporphyrinogen III synthase:Molecular basis of congenita...;52
6.1;I. Introduction;53
6.2;II. Uroporphyrinogen III Synthase;56
6.3;III. Molecular Basis of CEP;63
6.4;IV. The Hotspot Mutation C73R-UROIIIS;71
6.5;V. Treatment of CEP;75
6.6;VI. Concluding Remarks;78
6.7;Acknowledgments;79
6.8;References;80
7;Chapter 3: Role of Fibrin Structure in Thrombosis and Vascular Disease;84
7.1;I. Introduction;85
7.2;II. The Coagulation Cascade;86
7.3;III. Fibrinogen Structure and Function;90
7.4;IV. Factor XIII Structure and Function;93
7.5;V. Clot Formation and Function;95
7.6;VI. Fibrinolysis;100
7.7;VII. Elastic Properties of Fibrin;103
7.8;VIII. Heterogeneity in Coagulation and Fibrin Structure;105
7.9;IX. Environmental Factors and Fibrin Structure;111
7.10;X. Fibrin Density and Thrombosis;114
7.11;XI. Interactions with Cells and Wound Healing;116
7.12;XII. Perspectives;118
7.13;References;119
8;Chapter 4: Structural, dynamic, and functional aspects of helix association in membranes...;138
8.1;I. Introduction;139
8.2;II. Prediction of Structure of HH Dimers;142
8.3;III. Free Energy of TM Helix-Helix Association;150
8.4;IV. Combination of Modeling and Experimental Techniques;155
8.5;V. Limitations and Shortcomings of the Computational Methods;157
8.6;VI. Comparison with NMR Models: How Reliable Is The Reference?;159
8.7;VII. Is an Accurate Structure Prediction Always Required?;160
8.8;VIII. What Makes TM Helices Suitable Pharmacological Targets?;161
8.9;IX. Modeling of TM Helical Dimers as a First Step Toward 3D Structure of Polytopic MPs;161
8.10;X. From Structure and Thermodynamics to Function and Design;162
8.11;XI. Conclusion;163
8.12;Acknowledgments;164
8.13;References;164
9;Chapter 5: Proteins MOVE! Protein dynamics and long-range allostery in cell signaling;172
9.1;I. Introduction;173
9.2;II. NHERF1 Modulates the Macromolecular Assembly, Cell Surface Retention, and Subcellular Localization of Membrane Proteins...;176
9.3;III. Signal Transduction by Allosteric Scaffolding Protein Interactions;180
9.4;IV. Structural Basis of Autoinhibition and Long-Range Allostery in NHERF1;187
9.5;V. Dynamic Propagation of Allosteric Signals by Nanoscale Protein Motion;195
9.6;VI. Summary and Perspective;222
9.7;Acknowledgments;222
9.8;References;223
10;Chapter 6: Structural diversity of class I MHC-like molecules and its implications in binding specificities;232
10.1;I. Introduction;233
10.2;II. Sequence Analysis;236
10.3;III. Structure Analysis;248
10.4;IV. Glycosyalation;267
10.5;V. Conclusion;270
10.6;Acknowledgments;270
10.7;References;271
11;Author Index;280
12;Subject Index;306
13;Colour Plate;314