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In this book, renowned scientists describe how cholesterol interacts with various proteins. Recent progress made in high-resolution visualization of cholesterol-protein interactions using crystallography and cryogenic electron microscopy has substantially advanced the knowledge of critical features that enable specific recognition of the cholesterol molecule by proteins that was built on earlier studies using binding assays, computational modeling and site-directed mutagenesis. This book offers comprehensive insights into the current understanding of cholesterol-driven modulation of protein function via direct sensing. In the first part, the chapters introduce the reader to the general characteristics of cholesterol binding sites in proteins. This part starts with a tour into common cholesterol recognition motifs that have been elucidated up-to-date followed by an overview of the major classes of steroid-binding proteins. It then continues to two chapters that present a comprehensive analysis of molecular and structural characteristics of cholesterol binding sites in transmembrane and soluble protein domains. In the second part of the book, examples of cholesterol-binding sites and consequences of specific cholesterol recognition for protein function are presented for G protein-coupled receptors, ion channels and cholesterol-transporting proteins. The book will be of interest to undergraduate and graduate students, as well as basic science and medical researchers with a keen interest in the biophysical properties of cholesterol and physiological consequences of cholesterol presence in biological systems.