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Naturally Occurring Polymers—Animals
Published in Charles E. Carraher, Carraher's Polymer Chemistry, 2017
Membrane proteins are attached to or associated with the membrane of a cell. More than half of the proteins interact with these membranes. Membrane proteins are generally divided according to their attachment to a membrane. Transmembrane proteins span the entire membrane. Integral proteins are permanently attached to only one side of membranes. Peripheral membrane proteins are temporarily attached to integral proteins or lipid bilayers through combinations of noncovalent bonding such as hydrophobic and electrostatic bonding. These membranes often act as receptors or provide channels for charged or polar molecules to pass through them.
Potential of Microalgae for Protein Production
Published in Sanjeet Mehariya, Shashi Kant Bhatia, Obulisamy Parthiba Karthikeyan, Algal Biorefineries and the Circular Bioeconomy, 2022
Elena M. Rojo, Alejandro Filipigh, David Moldes, Marisol Vega, Silvia Bolado
Proteins may be found within the plasma membrane and in the cell wall (as transmembrane proteins), or bound to the membrane's lipids (as periphery proteins) (Figure 4.2). They are also found in the cytoplasm or as part of many organelles such as chloroplast, mitochondria, the endoplasmic reticulum, or inside the cell's nucleus (Safi et al., 2014a). Transmembrane proteins have a hydrophobic region in contact with the bilayer membrane that is tightly bound (Safi et al., 2014a).
Challenges of expressing recombinant human tissue factor as a secreted protein in Pichia pastoris
Published in Preparative Biochemistry & Biotechnology, 2022
Mohammad Jalili-Nik, Mohammad Soukhtanloo, Majid Mojarrad, Mohammad Hadi Sadeghian, Baratali Mashkani
Membrane proteins contain a hydrophobic transmembrane region. It was previously reported that the total hydrophobicity of the signal secretion signal is an important factor influencing protein secretion efficiency Fitzgerald and Glick[16], Peng et al.[23] Sequence analysis of TF using Kyte and Doolittle hydrophobicity plots (ExPasy, http:\\www.expasy.ch\cgi-bin\protscale.pI) revealed that its transmembrane region is highly hydrophobic (Figure 7) Kyte and Doolittle.[24] The hydrophobicity of expressed proteins favors their integration into the lipid bilayer of the intracellular membrane, thereby leading to inefficient translocation and ER export. Thus, the hydrophobicity of the TED region in TF proteins might be contributed to the failure in its proper trafficking and secretion.
Plant pharmacology: Insights into in-planta kinetic and dynamic processes of xenobiotics
Published in Critical Reviews in Environmental Science and Technology, 2022
Tomer Malchi, Sara Eyal, Henryk Czosnek, Moshe Shenker, Benny Chefetz
Transmembrane receptors within cytosolic domains cause enzyme activation or modification of the influx/efflux of endogenous compounds. Transmembrane proteins with domains on both sides of the membrane are poised structurally to transmit information from one side of the membrane to the other. Plant proteins have been identified that resemble the receptor protein kinases of animal cells, known as receptor-like protein kinases (Braun & Walker, 1996; He et al., 2018). In addition to receptor activity, xenobiotics compounds may modify cell membrane structure and function (Page & Maddison, 2008; Wink, 2010).
Inhibitory effects of intact silkworm sericin on bacterial proliferation
Published in The Journal of The Textile Institute, 2021
Erica Matsumoto, Keiko Takaki, Rina Maruta, Hajime Mori, Eiji Kotani
Our results also showed that intact sericin affected the colony size of E. coli and S. enterica, but had no effect on colony growth in S. aureus and B. subtilis (Figures 2 and 3; Table 2). E. coli and S. enterica are examples of Gram-negative bacteria, which have the outer membrane outside the cell wall, with a thin peptide glycan layer. Their outer membrane is a lipid bilayer composed of phospholipids, lipopolysaccharides, and transmembrane lipoproteins, such that hydrophilic molecules can move in and out of the cell body through pores (Silhavy et al., 2010; Nikaido, 2003). However, unlike Gram-negative bacteria, Gram-positive bacteria, including S. aureus and B. subtilis, have a thicker peptide glycan layer, which is a very thick network structure consisting of N-acetyl glucosamine and N-acetyl muramic acid (Silhavy et al., 2010). It is known that higher metabolic activities are necessary to actively import higher molecular weight substances through this thick peptide glycan layer than through the thinner layer associated with Gram-negative bacteria (Silhavy et al., 2010, p. 15; Meroueh et al., 2006). Thus, the lack of an effect of sericin on the growth of Gram-positive bacteria is likely due to the thick peptide glycan layer outside the cytoplasmic membrane of these bacteria, which would hinder the passage of sericin proteins of varying molecular sizes (Figure 1). The amino acid composition of intact sericin and the degraded commercial sericin were shown to be very similar (Table 1), although the results from SDS-PAGE showed quite different banding patterns (reflecting differences in size) between intact sericin and the degraded sericin (Figure 1). The intact sericin slowed the growth in Gram-negative bacteria, suggesting the importance of the high molecular weight proteins in intact sericin solution.