Membrane-induced conformational change of proteins.
Many proteins exhibit both a water-soluble and a membrane-bound state. The proteins in the membrane-bound state obtain a distinct structure from that in the bulk, which exists in many important biological processes. In the present paper we would stress that the variation of the physical chemistry properties of the microenvironment adjacent to the membrane-surface region play an important role in the process of the membrane-induced conformational changes of the proteins.
Sui
S F
SF
Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, People's Republic of China. suisf@mail.tsinghua.edu.cn
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003087:Colicins / Q000737:chemistry / Q000187:drug effects; D006023:Glycoproteins / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008051:Lipid Bilayers / Q000737:chemistry; D008555:Melitten / Q000737:chemistry; D008563:Membrane Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008956:Models, Chemical; D010743:Phospholipids / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D012995:Solubility; D015978:Trichosanthin / Q000737:chemistry; D014508:Urea / Q000494:pharmacology; D053482:beta 2-Glycoprotein I
D003087:Colicins; D006023:Glycoproteins; D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins; D010743:Phospholipids; D053482:beta 2-Glycoprotein I; D008555:Melitten; D015978:Trichosanthin; D014508:Urea