![]() ![]() ![]() By the start of the 1980’s the complexity of protein structures had been simplified through the systematic development and use of schematic ribbon drawings to illustrate the then approximately 75 known protein structures and in its essence remains the most popular way to visualize these highly complex forms today. This view was originally and most obviously conceived when the first 3D structures were being determined by John Kendrew, Max Perutz, Dorothy Hodgkin and other early crystallographers in the 1950’s, 60’s and 70’s. Protein structures have been traditionally viewed as constructs of secondary structure which pack into a 3D arrangement. There are also a small group of proteins which are intrinsically unstructured and these disordered proteins are gaining considerable attention in biochemistry for their unique structural and functional properties. They are also integral constituents of membranes and as peripheral or integral membrane proteins play a pivotal role in controlling the transport of metabolites into and out of the cell, serve as receptors, adhesion molecules as well as participate in cell–cell communication. ![]() The protein α-keratin for example is found in hair and fingernails and collagen is found in connective tissue which composes cartilage, bones and blood vessels. Proteins are also found in less-soluble fibrous forms that compose key structural elements. Soluble, globular proteins have many function including transporting molecules such as oxygen, lipids and odorants, fighting foreign invaders such as bacteria and viruses to protect the organism, catalyzing reactions in metabolic pathways that are central to catabolism and anabolism, transcribing and translating DNA and RNA respectively, and generating signaling cascades, to name just a few critical roles. Proteins are the building blocks of almost all biological processes that constitute life. Protein structure, protein folding, long-range interactions, allostery, networks, graph theory INTRODUCTION ![]()
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