Transmembrane proteins—Different anchoring systems

Abstract

Transmembrane proteins are active in amphipathic environments. To stabilize the protein in such surrounding the exposure of hydrophobic residues on the protein surface is required. Transmembrane proteins are responsible for the transport of various molecules. Therefore, they often represent structures in the form of channels. This analysis focused on the stability and local flexibility of transmembrane proteins, particularly those related to their biological activity. Different forms of anchorage were identified using the fuzzy oil‐drop model (FOD) and its modified form, FOD‐M. The mainly helical as well as β‐barrel structural forms are compared with respect to the mechanism of stabilization in the cell membrane. The different anchoring system was found to stabilize protein molecules with possible local fluctuation.

Editorial: Structure and function of trans-membrane proteins

“…One of the peculiarities of these proteins is the problem of the influence of the external force field on the folding process. Indeed, the polar environment of water pushes hydrophobic residues towards the central zone of the protein, forming a hydrophobic core ( Roterman et al, 2023 ). In contrast, the membrane environment pushes hydrophobic residues towards the protein surface ( White and von Heijne, 2004 ).…”