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Structural Biochemistry/Membrane Proteins - Wikibooks, open books for an open world. A membrane protein is any protein found in a biological membrane. They participate in various biological processes, such as cell signaling- transduction pathways. The membrane proteins also play a strong role in controlling a wide array of gradients such as chemical, electrical, and mechanical gradients and are responsible for cell structure during key cell events such as division. Due to their many functions in the membrane, they are in high concentration on the surface of the membrane. They may also act as channels that move specific molecules into and out of the membrane. Membrane proteins are proteins that interact with, or are part of, biological membranes. They include integral membrane proteins that are permanently anchored or part of the membrane and peripheral membrane proteins that are. A membrane protein is any protein found in a biological membrane. They participate in various biological processes, such as cell signaling-transduction pathways. The membrane proteins also play a strong role in controlling a.
Theses proteins fall into two main categories, depending upon how strongly the protein interacts with the membrane. The two main categories are listed below: Integral proteins: (also called intrinsic proteins) These are proteins are characterized by strong interaction with the membrane, which can only be broken by the addition of detergents or some other nonpolar solvent. Essentially, they are permanently bounded to the membrane. They may span across the entire phospholipid bi- layer, or be monotopic. Most integral proteins contain residues with hydrophobic side chains that interact with fatty acyl groups of the membrane phospholipids, thus anchoring the protein to the membrane. Most integral proteins span the entire phospholipid bilayer. It interacts extensively with the hydrocarbon chain of membrane lipid and they can be released by agents that compete for these nonpolar interaction. Peripheral proteins: (or extrinsic proteins) are proteins that have a much weaker interaction with the membrane than integral proteins. These attachments tend to be much more temporary and can be displaced via treatment with a polar reagent. This type of proteins does not interact with the hydrophobic core of the phospholipid bilayer. They are usually bound to membrane by interactions with integral membrane proteins or directly by interactions with lipid polar head groups. This polar interaction can be disrupted by the change in p. H. There is also an alternative method of classification for membrane proteins. It arises from membrane proteins, such as colicin A and alpha- hemolysin. These do not fit to either integral or peripheral classification. The functioning of biological membrane proteins (MPs) within synthetic block copolymer membranes is an intriguing phenomenon that is believed to offer great potential for applications in life and medical sciences and. The lysosome is a central, acidic organelle that is involved in the degradation of macromolecules through the activity of lysosomal hydrolases. Lysosomes are crucial. In this alternative system of classification, the membrane proteins are divided into integral and amphitropic. Biological membranes have phospholipid bilayer structure which contains a set of proteins which help plasma membrane to carry its distinctive functions. Membrane proteins can be attached to the membrane or associated with the membrane of a cell or an organelle. Membrane proteins can be classified into two groups based on the strength of their association with the membrane: Some membrane proteins are found bounded to lipid bilayer and generally involved in cell- cell signaling or interactions. Others are embedded within the lipid bilayer of a cell often form channels and pores. Membrane proteins can be attached to both the outside and inside of the cell membrane. Proteins can be attached to the cell membrane in a variety of ways. One method involves irreversible covalent modification. Both Ras (a GTPase) and Src (protein tyrosine kinase) are known to be modified in this manner. Both of these proteins participate in signal transduction pathways, but upon covalent attachment of a lipid group they become attached to the inner face of the cytoplasmic membrane. When Ras and Src are affixed to the cell membrane they are better able to receive and transmit information being transferred via their respective signal transduction pathways. Membrane proteins can be made of alpha helices or beta strands,or the combination of both alpha helices or beta strands. For example the channel protein called Porin is made up of entirely beta strands, while the enzyme protein called prostaglandin is made entirely of the alpha helices. Membrane proteins can be alpha - helices or beta - strands. Proteins can span the membrane with alpha helices. Membrane - spanning alpha - helices are the most common structural motif in membrane proteins. An examination of the primary structure reveals that most amino acids in the membrane protein are nonpolar and very few are charged. One of the first alpha - proteins found was the bacteriorhodopsin. It uses light energy to transport protons from inside the cell to outside generating a proton gradient used to form ATP. The seven alpha - helices are closely packed and arranged perpendicular to the plane of the cell and they span 4. A in width. Membrane proteins can also be made out of beta strands. Beta Strands form channel proteins. They are less common than alpha - helices. Channel proteins are formed by beta arrangement of beta strands. Each strand is hydrogen bonded to its neighbor in an anti- parallel arrangement, forming a single beta sheet. The beta sheet then curls up to form a hollow cylinder that forms a channel in the membrane. The outside surface is non- polar and interacts with the hydrocarbon core of the membrane, while the inside channel is hydrophillic and filled with water. The arrangement of polar and non- polar is accomplished by the alternation of hydrophobic and hydrophillic amino acids along with each beta strand. Many membrane proteins have quaternary structures consisting of multiple subunits. This oligomerization in membrane proteins is beneficial to their functions, stability, genetic efficiency and maybe even optimizing productive output per unit area of the membrane. Cytochrome b. 6f serves as an example of quarterary structure affecting membrane protein function. This protein consist of two subunits which are connected by a bridge so that electrons can be transferred between them. As for stability, a quaternary protein consisting of 2, 3 or 4 subunits would be 2, 3 or 4 times more stable if a stability improving mutation were to occur on each subunit. It would be more genetically efficient to have all the subunits of a quaternary protein be coded for by 1 gene than to have each of its subunits be coded for by a different gene. In this way, a quaternary protein can be coded for with minimal genetic space. One example of this are the ion channels that span the membrane. Everyone of these subunits and therefore the iono channel as a whole, is then coded by and translated from 1 single gene. In addition, oligomerization may also contribute to maximizing functional output as it allows membrane proteins to be closely packed in an area of the lipid bilayer without coming into contact with other proteins in energetically unfavorable ways. When the presence of a mutation is detected a small protein named ubiquitin is attached to the damaged protein; this modification signals that the marked protein is to be destroyed. It is essential that the protein be destroyed before anaphase so that the damaged DNA is not passed on to other cells. The attachment of ubiquitin to a damaged protein is the first step of apoptosis, which is programmed cell death. One or more parts of these proteins are embedded in the phospholipid bi- layer of the membrane. They exhibit strong interaction with the membrane because their amino acid residues contains hydrophobic side chains that interact with the hydrophobic interior (fatty acyl groups) of the phospholipid bilayer. Because of their strong hydrophobic interaction with the hydrophobic core of the membrane, such proteins can only be dissociated from the membranes using detergents, non- polar solvents, or sometimes denaturing agents. Lastly, it is important to note that integral proteins account for a significant fraction of the proteins encoded in the genome. There are two basic categories for integral proteins. Transmembrane proteins. They are the most common among integral proteins. They may cross the membrane only once or several times, weaving in and out. The two kinds of transmembrane proteins are alpha- helical and beta- barrels. The former is the more common of the two and can be found in the inner membrane of bacterial cells or the plasma membrane of eukaryotes. Voltage- gated ion channels, such as potassium and chloride channels, are examples of alpha- helical transmembrane proteins. They are mostly composed of hydrophobic amino acid residues and little hydrophilic residues, such as charged and polar residues. The polar carbonyl oxygen in the backbone doesn. Van der Waals interactions hold the tertiary and quaternary structures together in the transmembrane region. These interactions allow for flexibility in the structure to accommodate for necessary functions. Two polar residues that are found most frequently in the TM backbone are serine and threonine which can potentially hydrogen bond to the helical backbone. This hydrogen bonding captures polar side chains in a hydrophobic environment, such as a lipid bilayer. The polar side chains in turn hydrogen bond to other helices. Two residues, glycine and proline, known as helix breakers in water make kinks in the helix which play significant roles in functional mechanisms. Porins are examples of a beta- barrel transmembrane protein. They cross cellular membrane and acts as a pore through which molecules can diffuse. Transmembrane proteins can further be categorized into Type I and Type II. In Type I, the N- terminal is positioned on the exterior of the membrane. In Type II, the C- terminal appears on the exterior of the membrane. VDAC (voltage- dependent anion channel) is an example of a transmembrane protein found in the mitochondrial outer membrane which provides the pore for substrate diffusion. VDAC is composed of 1. This helps to solve the membrane topology of VDAC and gives the first eukaryotic . Something different about this integral membrane protein was that it had parallel . 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