Exploring the World of Membrane Proteins: Techniques and Methods for Understanding Structure, Function, and Dynamics

Abstract

In eukaryotic cells, membrane proteins play a crucial role. They fall into three categories: intrinsic proteins, extrinsic proteins, and proteins that are essential to the human genome (30% of which is devoted to encoding them). Hydrophobic interactions inside the membrane serve to stabilize integral proteins, which span the lipid bilayer. This review investigates a number of computational and experimental methods used to study membrane proteins. It encompasses a variety of technologies, including electrophoresis, X-ray crystallography, cryogenic electron microscopy (cryo-EM), nuclear magnetic resonance spectroscopy (NMR), biophysical methods, computational methods, and artificial intelligence. The link between structure and function of membrane proteins has been better understood thanks to these approaches, which also hold great promise for future study in the field. The significance of fusing artificial intelligence with experimental data to improve our comprehension of membrane protein biology is also covered in this paper. This effort aims to shed light on the complexity of membrane protein biology by investigating a variety of experimental and computational methods. Overall, the goal of this review is to emphasize how crucial it is to understand the functions of membrane proteins in eukaryotic cells. It gives a general review of the numerous methods used to look into these crucial elements and highlights the demand for multidisciplinary approaches to advance our understanding.

Fundamental Mechanisms in Membrane Receptology: Old Paradigms, New Concepts and Perspectives

“…Indeed, the specific lipid requirement of membrane protein is considered a bottleneck for heterologous expression [39]. It is also a major consequence of the epigenetic dimension of protein structure (EDPS) [40][41][42], a concept developed for explaining the failure of the AlphaFold algorithm [40,43] for correctly predicting the structure of membrane proteins from their amino acid sequence [41,42,44,45].…”

Membrane Proteins in Action Monitored by pH-Responsive Liquid Crystal Biosensors

“…In the human body, one-third of all proteins are membrane proteins, which are the target of more than 60% of modern drugs . The study of membrane proteins is challenging due to their instability when isolated from their native environment, though they have been intensively studied by X-ray crystallography, single-particle cryoelectron microscopy (cryo-EM), receptor–ligand binding assays, etc . However, to the best of our knowledge, LC biosensors have not been demonstrated for studying membrane proteins.…”