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What are indentations on the surface of a plasma membrane that contain receptor proteins?
coated pits. :)
What does the membrane contain?
ions,phospholipids,carbohydrates,proteins,cholesterol,glycoproteins
Does plasma membrane produce proteins?
No, the plasma membrane does not produce proteins. Proteins are synthesized by ribosomes in the cytoplasm and then transported to the plasma membrane to carry out various functions such as transport, signaling, and cell adhesion.
Glycoproteins are membrane proteins?
Yes they are found as integral membrane proteins in addition to lipidis, glycerol and proteins alone. Glycoproteins are proteins that are post translationally coneected to sugar chains. Mostly the secreted proteins are also glycoslated.
What is the similarities between enzyme and hormone?
Both enzymes and receptors have specific sites for the substrates to bind. The receptor causes a response beyond the cell membrane and the enzyme facilitates a chemical change in the substrate. Enzymes can be membrane bound or free floating. Receptors are usually membrane proteins
Cell contains receptor proteins for various chemicals?
Receptor proteins on the cell surface bind to specific chemicals, triggering intracellular signaling pathways that initiate cellular responses. These responses can include changes in gene expression, enzyme activity, or cell behavior based on the type of chemical detected by the receptor. This process plays a critical role in cell communication, regulation, and homeostasis.
What receptor cells are in mucous membrane?
Mucous membranes contain various types of receptor cells, including pain receptors (nociceptors), temperature receptors (thermoreceptors), and chemical receptors (chemoreceptors). These receptor cells help the body sense and respond to different stimuli in the environment.
What does cell membrane contain?
It contains proteins, which are ribosomes, and the E.R.YHURRR WELCOME!!!! I'm mean please say thanks :)
You could locate receptor sites involved in transmiting a nerve impulse by finding the?
Synapse? Dendrite? Dendritic spine? Or, "You could maybe a better answer to your question get if you re-stated it less confusingly as?" ie, perhaps, "Where are the receptor sites involved in transmitting a nerve impulse LOCATED?"
What send proteins to the Golgi apparatus?
Proteins are sent to the Golgi apparatus from the endoplasmic reticulum in vesicles that bud off from the ER membrane. These vesicles contain the proteins in transport to the Golgi for further processing and sorting.
Which organelle does not contain a partially permeable membrane?
The ribosome is an organelle that does not contain a partially permeable membrane. Unlike membrane-bound organelles such as the nucleus or mitochondria, ribosomes are composed of ribosomal RNA and proteins, and they exist freely in the cytoplasm or attached to the endoplasmic reticulum. They function in protein synthesis without the need for a membrane structure.
What is the structure of receptor proteins?
Receptors are plasma membrane proteins that bind specific molecules, e.g., growth factors, hormones, or neurotransmitters, and then transmit a signal to the cell's interior that causes the cell to respond ina aspecific manner, a process called signal transduction cascade.There are several types of receptor proteins grouped in families of transmembrane proteins. For some families of important membrane proteins, e.g., ion channel proteins, the hydropathy plots (those that help to predict the hydrophobic regions of a membrane protein according to its amino acid sequence and hydropathic index) is often not very reliable because that the membrane-spanning regions of these proteins from channels in the membrane while on the other hand they need hydrophilic residues to line the surface of the channels in contact with the aqueous phase. These are the most important and most well-known receptor-protein families:Receptor Protein-Tyrosine Kinases. Known as RPTKs, are type I transmembrane proteins, with their N-termini outside of the cell and single membrane-spanning regions. The structural features that are the transmembrane domain that divides the molecule into a ligand-binding domain and a cytoplasmic domain that contains a conserved protein kinase catalytic domain. On the outside, the N-terminal end, RPTK has a signal peptide that ensures that the protein will be targeted to the secretory pathway. This is followed by an extracellular domain of several hundred amino acids that contain N-linked glycosilation sites, a distintive pattern of cysteine residues, and often a characteristic array of structural motifs. The transmembrane domain consists of about 24 hydrophobic residues that are usually succeeded by several basic residues that function as a stop-transfer signal. On the cytoplasmic side of the membrane there is a juxtamembrane region, usually of around 50 residues long, and which in some cases is known to have important regulatory functions. Next follows the catalytic domain, which is related to the catalytic domains of the cytoplasmic protein-tyrosine kinases and the protein-serine/threonine kinases, and is about 250 residues in length, excluding inserts. The phospho-transfer function lies entirely whithin this region. The region C-terminal to the catalytic domain is of variable length and can be up to 200 residues. The functions of this C-terminal tail vary among members of the RPTKs. Exmaples of this kind of receptors are: EGFR (Epidermial Growth Factor Receptor), PDGFR (Platelet-Derived Growth Factor Receptor), IR (Insulin Receptor), NGFR (Nerve Growth Factor Receptor), FGFR (Fibroblast Growth Factor Receptor), etc.G proteins. Several important physiological responses like vision, smell, and stress response produce large metabolic effects from a small number of input signals. The receptors for these signals have two things in common, first, they are transmembrane proteins with seven helices spanning the lipid bilayer of the plasma membrane, and second, the signals received by these receptors are amplified and the amplifiers are members of a common family of proteins called G proteins. Most G proteins are heterotrimers consisting of a one copy of alpha (45 kD), beta (35 kD), and gamma (7 kD) subunits. The alpha subunits have GTPase activity and slowly hydrolyze GTP to GDP and inorganic phosphate. The GTP-bound form of the protein is the active form and sends a signal from the receptor to some cellular effector protein. Examples of these kind of receptors are: beta-adrenergic receptor, rhodopsin, mast cell IgE receptor, and muscarinic receptor.
