Protein-Protein Interactions (PPIs): Types, Methods for Detection and Analysis

Clyde R. Montgomery (Editor)

Series: Biochemistry Research Trends
BISAC: SCI007000



Volume 10

Issue 1

Volume 2

Volume 3

Special issue: Resilience in breaking the cycle of children’s environmental health disparities
Edited by I Leslie Rubin, Robert J Geller, Abby Mutic, Benjamin A Gitterman, Nathan Mutic, Wayne Garfinkel, Claire D Coles, Kurt Martinuzzi, and Joav Merrick


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Protein-protein interactions (PPIs) play an important role in vital biological processes such as metabolic and signaling pathways, cell cycle control, and DNA replication and transcription. This book discusses types, methods for detection and the analysis of PPIs. Chapter One describes two key nuclear magnetic resonance (NMR) methods for the investigation of protein-protein interactions, chemical shift perturbation, and residual dipolar coupling, with practical tips on the preparation of samples, NMR measurement, and analysis. Chapter Two describes the basic principles and provides a practical description of the recent technological developments in solution NMR spectroscopy for examining protein-protein interactions. Chapter Three focuses on identifying PPIs via many learning methods based on protein sequence information. Chapter Four examines the thermodynamics of PPIs by isothermal titration calorimetry. Chapter Five describes the general microscopic features of amyloid fibril structures and then discusses the macroscopic properties of protein aggregate with conformations such as packing, hydration, and enthalpy using thermodynamic variables in combination with densitometry and isothermal titration calorimetry. Chapter Six reviews the special case of protein self-association as a modulator of protein function. (Imprint: Nova)


Chapter 1. Advanced Techniques to Detect Protein–Protein Interactions using Solution Nuclear Magnetic Resonance. Part I: Chemical Shift Perturbation and Residual Dipolar Coupling
Young-Ho Lee and Toshihiko Sugiki (Institute for Protein Research, Osaka University, Suita, Osaka Prefecture, Japan)

Chapter 2. Advanced Techniques to Detect Protein-Protein Interactions using Solution Nuclear Magnetic Resonance. Part II: Cross-Saturation, Paramagnetic Effects, and In-Cell NMR
Toshihiko Sugiki and Young-Ho Lee (Institute for Protein Research, Osaka University, Suita, Osaka Prefecture, Japan)

Chapter 3. Identifying Protein-Protein Interactions via Many Learning Methods Based on Protein Sequence Information
Yijie Dinga, Jijun Tangb and Fei Guo (School of Computer Science and Technology, Tianjin University, Tianjin, P.R.China, and others)

Chapter 4. Thermodynamics of Protein-Protein Interactions Examined by Isothermal Titration Calorimetry
Ju Yaen Kim, Misaki Kinoshita, Takashi Inui, Genji Kurisu, Yuji Goto, Toshiharu Hase, Koichiro Ishimori and Young-Ho Lee (Institute for Protein Research, Osaka University, Osaka, Japan, and others)

Chapter 5. Molecular Structure of Amyloid Fibrils Revealed by Thermodynamics
Tatsuya Ikenoue, Yuxi Lin, Misaki Kinoshita, Kazumasa Sakurai, Yuji Goto, and Young-Ho Lee (Institute for Protein Research, Osaka University, Osaka, Japan, and others)

Chapter 6. Protein Self-Interaction in Health and Disease: How Dimerization, Oligomerization and Polymerization Modulate Protein Function
Ailis O’Carroll, Mehdi Moustaqil, Andre Goulart-Leitao, Yann Gambin, and Emma Sierecki (EMBL Australia Node in Single Molecule Science and School of Medical Sciences, Faculty of Medicine, University of New South Wales, Kensington, Australia)


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