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For example, the "unfolded" bacteriorhodopsin in SDS micelles has four transmembrane α-helices folded, while the rest of the protein is situated at the micelle-water interface and can adopt different types of non-native amphiphilic structures. Free energy differences between such detergent-denatured and native states are similar to stabilities ...
A transmembrane domain (TMD, TM domain) is a membrane-spanning protein domain.TMDs may consist of one or several alpha-helices or a transmembrane beta barrel.Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues.
The protein can broadly be split into the Notch extracellular domain (NECD) and Notch intracellular domain (NICD) joined together by a single-pass transmembrane domain (TM). The NECD contains 36 EGF repeats in Drosophila , [ 13 ] 28-36 in humans, and 13 and 10 in C. elegans Lin-12 and GLP-1 respectively. [ 27 ]
Tetraspanins are a family of membrane proteins found in all multicellular eukaryotes also referred to as the transmembrane 4 superfamily (TM4SF) proteins. These proteins have four transmembrane alpha-helices and two extracellular domains, one short (called the s mall e xtracellular d omain or l oop, SED/SEL or EC1) and one longer, typically 100 ...
10972 100042773 Ensembl ENSG00000170348 ENSMUSG00000114251 UniProt P49755 n/a RefSeq (mRNA) NM_006827 XM_036158265 RefSeq (protein) NP_006818 n/a Location (UCSC) Chr 14: 75.13 – 75.18 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Transmembrane emp24 domain-containing protein 10 is a protein that in humans is encoded by the TMED10 gene. This gene is a member of the EMP24/GP25L ...
The membrane-spanning segments, designated S1-S6, all take the form of alpha helices with specialized functions. The fifth and sixth transmembrane segments (S5 and S6) and pore loop serve the principal role of ion conduction, comprising the gate and pore of the channel, while S1-S4 serve as the voltage-sensing region.
The MIP family is large and diverse, possessing thousands of members that form transmembrane channels. These channel proteins function in transporting water, small carbohydrates (e.g., glycerol), urea, NH 3, CO 2, H 2 O 2 and ions by energy-independent mechanisms.
A recent review discusses evidence regarding the structure and function of claudin family proteins using a systems approach to understand evidence generated by proteomics techniques. [13] A chimeric claudin was synthesized to help enhance the understanding of both the structure and function of the tight junction. [14]