Transmembrane Domain
Transmembrane Domain - Related Videos
06:45
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Cited by 7 •
2011
An efficient procedure to assess the oligomerization propensity of single-pass transmembrane domains (TMDs) is described. Chimeric proteins consisting of the TMD fused to ToxR are expressed in an E. coli reporter strain. TMD-induced oligomerization causes dimerization of ToxR, activation of transcription and production of the reporter protein, -galactosidase.
12:05
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Cited by 7 •
2013
Biophysical and biochemical studies of interactions among membrane-embedded protein domains face many technical challenges, the first of which is obtaining appropriate study material. This article describes a protocol for producing and purifying disulfide-stabilized transmembrane peptide complexes that are suitable for structural analysis by solution nuclear magnetic resonance (NMR) and other analytical applications.
02:26
Conservation of Protein Domains Over Different Proteins
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2020
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms. A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
09:26
Optical Mapping of Intra-Sarcoplasmic Reticulum Ca2+ and Transmembrane Potential in the Langendorff-perfused Rabbit Heart
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Cited by 8 •
2015
This article describes the detailed protocol and equipment necessary for dual optical mapping of transmembrane potential (Vm) and free intra-sarcoplasmic reticulum (SR) Ca2+ in the Langendorff-perfused rabbit heart. This method allows for direct observation and quantification of Vm and SR Ca2+ dynamics in the intact heart.
01:25
Single-pass Transmembrane Proteins
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2023
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
FAQs
An alpha helix allows nonpolar amino acid side chains to interact with surrounding membrane lipids while the peptide backbone remains stabilized by internal hydrogen bonds. This arrangement supports passage through the lipid bilayer and helps maintain the structural integrity of the membrane-spanning region. The resulting architecture is central to how membrane proteins remain positioned across membranes.
Its position within a protein helps establish which portions of that protein lie on different sides of a cell or organelle membrane. Because transmembrane domains span the bilayer, they provide a structural framework for defining protein orientation and topology. This organization is important when receptors, enzymes, or signaling proteins must operate in specific membrane locations.
Multiple transmembrane domains can form a coordinated membrane-spanning structure rather than acting only as a single anchor. Their assembly can produce channels or transporters, giving the protein an architecture suited to moving molecules across the membrane. This distinguishes multi-domain arrangements from simpler membrane attachments that primarily position receptors, enzymes, or signaling proteins.
They provide stable membrane anchoring while helping place the functional parts of a protein in the appropriate cellular environment. For receptors and signaling proteins, this positioning supports membrane-based sensing and communication. For membrane-associated enzymes, anchoring keeps catalytic activity connected to the membrane. Thus, the domain contributes both structural placement and biological function.
Analysis can support predictions about whether a protein contains membrane-spanning regions and how those regions may position the protein. It can also help researchers investigate protein topology, meaning the arrangement of protein regions relative to the membrane. These insights are useful for interpreting the organization and potential roles of previously studied or newly examined membrane proteins.
Researchers apply these studies to protein prediction, membrane-trafficking investigations, drug-target research, and questions about how cells sense or move molecules across membranes. The same structural information can connect protein organization with cellular behavior, including receptor placement, signaling, and transport. This makes transmembrane domains relevant across molecular biology and cell biology rather than to one process alone.