Membrane Protein : Integral/Peripheral
... – Form hydrophilic pathways in the membrane – Water and certain ions can pass – Voltage-gated channels • Open or closed by changes in voltage across the membrane or by binding molecules • Eg. Muscle contractions ...
... – Form hydrophilic pathways in the membrane – Water and certain ions can pass – Voltage-gated channels • Open or closed by changes in voltage across the membrane or by binding molecules • Eg. Muscle contractions ...
exploring protein structure
... strong ionic bonds between R groups with positive and negative charges, and ...
... strong ionic bonds between R groups with positive and negative charges, and ...
Supplementary Information
... Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. ...
... Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. ...
6Communication
... docking sites for proteins (A, B, C, and D) that interact with the activated PDGF-receptor. Binding of PDGF activates the PDGF-receptor leading to an increase in DNA synthesis. To determine whether protein A, B, C, and/or D are responsible for activation of DNA synthesis, you construct mutant versio ...
... docking sites for proteins (A, B, C, and D) that interact with the activated PDGF-receptor. Binding of PDGF activates the PDGF-receptor leading to an increase in DNA synthesis. To determine whether protein A, B, C, and/or D are responsible for activation of DNA synthesis, you construct mutant versio ...
Objectives 25
... GROWTH FACTORS AND SIGNAL TRANSDUCTION - cells require growth factor hormones to proliferate; absence of GF normal cells arrest at R-point of cell cycle; add GF (EGF) DNA replication Growth factor-receptor interaction - peptide GF bind to receptors which contain tyrosine kinase domains; these ki ...
... GROWTH FACTORS AND SIGNAL TRANSDUCTION - cells require growth factor hormones to proliferate; absence of GF normal cells arrest at R-point of cell cycle; add GF (EGF) DNA replication Growth factor-receptor interaction - peptide GF bind to receptors which contain tyrosine kinase domains; these ki ...
Signaling Through Scaffold, Anchoring, and Adaptor Proteins
... (12), indicating that PTB domains are principally peptide recognition elements, unlike SH2 domains that appear devoted to the job of pTyr recognition. PDZ domains have a somewhat similar mechanism of ligand-binding to PTB domains, in which the peptide binds as an additional strand to an antiparallel ...
... (12), indicating that PTB domains are principally peptide recognition elements, unlike SH2 domains that appear devoted to the job of pTyr recognition. PDZ domains have a somewhat similar mechanism of ligand-binding to PTB domains, in which the peptide binds as an additional strand to an antiparallel ...
Slide ()
... Vectorial discharge of a secretory polypeptide across the ER membrane mediated by a cleavable N-terminal insertion signal. The cotranslational passage of a polypeptide, such as a secretory or lysosomal protein, into the ER lumen is represented in a simplified form that does not include any molecular ...
... Vectorial discharge of a secretory polypeptide across the ER membrane mediated by a cleavable N-terminal insertion signal. The cotranslational passage of a polypeptide, such as a secretory or lysosomal protein, into the ER lumen is represented in a simplified form that does not include any molecular ...
A Brief Summary of Protein Targeting in Eukaryotes Or a brief
... Or a brief description of how certain eukaryotic proteins are targeted to the plasma membrane, extracellular matrix or cell wall, ER, vacuole, Golgi, chloroplast, mitochondrion, nucleus and cytoplasm. Note the special features (and sequences) associated with proteins that allow them to reach their p ...
... Or a brief description of how certain eukaryotic proteins are targeted to the plasma membrane, extracellular matrix or cell wall, ER, vacuole, Golgi, chloroplast, mitochondrion, nucleus and cytoplasm. Note the special features (and sequences) associated with proteins that allow them to reach their p ...
Manufacturing Muscle: Protein
... • Maintains bodily protein to prevent muscle tissue breakdown • Minimizes fatigue by providing branched-chain amino acids as fuel ...
... • Maintains bodily protein to prevent muscle tissue breakdown • Minimizes fatigue by providing branched-chain amino acids as fuel ...
Basics of protein structure Me Introduction to protein structure Four
... structure elements are connected ...
... structure elements are connected ...
Protein Targeting Notes
... Or a brief description of how certain eukaryotic proteins are targeted to the plasma membrane, extracellular matrix or cell wall, ER, vacuole, Golgi, chloroplast, mitochondrion, nucleus and cytoplasm. Note the special features (and sequences) associated with proteins that allow them to reach their p ...
... Or a brief description of how certain eukaryotic proteins are targeted to the plasma membrane, extracellular matrix or cell wall, ER, vacuole, Golgi, chloroplast, mitochondrion, nucleus and cytoplasm. Note the special features (and sequences) associated with proteins that allow them to reach their p ...
Poster - Protein Information Resource
... Name Rule Propagation Pipeline Affiliation of Sequence: Homeomorphic Family or Subfamily (whichever PIRSF is the lowest possible node) ...
... Name Rule Propagation Pipeline Affiliation of Sequence: Homeomorphic Family or Subfamily (whichever PIRSF is the lowest possible node) ...
Protein Trafficking4
... - tyr-based signals recruit μ subunits of AP2. - dileu-based signals recruit β subunits of AP2. - Arrestin binding to GPCRs facilitate receptor internalization by its ability to assocociate with clathrin and AP2. - Ubiquitin may recruit AP2 or clathrin, release the receptor from anchoring in the mem ...
... - tyr-based signals recruit μ subunits of AP2. - dileu-based signals recruit β subunits of AP2. - Arrestin binding to GPCRs facilitate receptor internalization by its ability to assocociate with clathrin and AP2. - Ubiquitin may recruit AP2 or clathrin, release the receptor from anchoring in the mem ...
Acrylamide -gel patterns of total soluble proteins at different stages +
... development (for instance the slow moving band, remaining near the cathode) while some other bands become visible in specific developmental stages; so the larval age can be recognized from the electrophoretic pettern of the larval proteins. At the end of the development it is possible to identify at ...
... development (for instance the slow moving band, remaining near the cathode) while some other bands become visible in specific developmental stages; so the larval age can be recognized from the electrophoretic pettern of the larval proteins. At the end of the development it is possible to identify at ...
Slide 1
... proteins that aggregate tend to collect – and are NEUROTOXIC. Note that these proteins ALSO aggregate in peripheral tissues, but are “cleared” and do not appear to be sufficiently toxic. ...
... proteins that aggregate tend to collect – and are NEUROTOXIC. Note that these proteins ALSO aggregate in peripheral tissues, but are “cleared” and do not appear to be sufficiently toxic. ...
Gene Section FGFR1 (Fibroblast Growth Factor Receptor 1) in Oncology and Haematology
... CEP110-FGFR1, and FIM-FGFR1; they encode large proteins containing the N-term of either FOP or CEP110, or FIM, and the catalytic domain of FGFR1 at their C-term: -N-term leucine-rich region from FOP fused to the catalytic domain of FGFR1; -N-term leucine zipper motifs from CEP110 fused to the cataly ...
... CEP110-FGFR1, and FIM-FGFR1; they encode large proteins containing the N-term of either FOP or CEP110, or FIM, and the catalytic domain of FGFR1 at their C-term: -N-term leucine-rich region from FOP fused to the catalytic domain of FGFR1; -N-term leucine zipper motifs from CEP110 fused to the cataly ...
12.4 G Protein–Coupled Receptors and Second Messengers
... catalytically active C subunits. This same basic mechanism—displacement of an autoinhibitory domain— mediates the allosteric activation of many types of protein kinases by their second messengers (as in Figs 12–7 and 12–23, for example). As indicated in Figure 12–12 (step 6 ), PKA regulates a number ...
... catalytically active C subunits. This same basic mechanism—displacement of an autoinhibitory domain— mediates the allosteric activation of many types of protein kinases by their second messengers (as in Figs 12–7 and 12–23, for example). As indicated in Figure 12–12 (step 6 ), PKA regulates a number ...
the ubiquitin system and a putative stimulatory role
... It is not entirely accurate to think of Ub as a simple tag, as Ub does appear to be involved in degradation. The proteasome is the structure that actually does the degrading. Ubiquiton's degradation role may simply be to decrease the rate of dissociation between proteasomes and interacting substrate ...
... It is not entirely accurate to think of Ub as a simple tag, as Ub does appear to be involved in degradation. The proteasome is the structure that actually does the degrading. Ubiquiton's degradation role may simply be to decrease the rate of dissociation between proteasomes and interacting substrate ...
The variable and conserved interfaces of modeled olfactory receptor
... segments, based on the rhodopsin two-dimensional projection map ~Scherlter et al., 1993!. Conserved residues in all the GPCRs ~Oliveira et al., 1993! are indicated. In addition, OR positions that align with ligand contact residues in other GPCRs are colored green; OR variable positions that do not a ...
... segments, based on the rhodopsin two-dimensional projection map ~Scherlter et al., 1993!. Conserved residues in all the GPCRs ~Oliveira et al., 1993! are indicated. In addition, OR positions that align with ligand contact residues in other GPCRs are colored green; OR variable positions that do not a ...
Molecular Machines (1MB429) Exam 2011-12-21
... Poly-A tail of mRNA is important for its efficient translation into protein. (a) How does poly-A tail participate in translation? What is the role of the PABP (PolyA Binding Protein) and initiation factor eIF4F in translation initiation? (eIF4F initiation factor contains eIF4E, eIF4A and MNK1 kinase ...
... Poly-A tail of mRNA is important for its efficient translation into protein. (a) How does poly-A tail participate in translation? What is the role of the PABP (PolyA Binding Protein) and initiation factor eIF4F in translation initiation? (eIF4F initiation factor contains eIF4E, eIF4A and MNK1 kinase ...
lecture notes endomembrane system 4
... is asymmetric. That is within the cell the carbohydrates are on the lumen side, and those on the plasma membrane therefore have the carbohydrate facing the outside of the cell. 14. What is the purpose of glycosylation? There is an important difference between the construction of an oligosaccharide a ...
... is asymmetric. That is within the cell the carbohydrates are on the lumen side, and those on the plasma membrane therefore have the carbohydrate facing the outside of the cell. 14. What is the purpose of glycosylation? There is an important difference between the construction of an oligosaccharide a ...
G protein–coupled receptor
G protein–coupled receptors (GPCRs), also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein–linked receptors (GPLR), constitute a large protein family of receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times.G protein–coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, and animals. The ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters, and vary in size from small molecules to peptides to large proteins. G protein–coupled receptors are involved in many diseases, and are also the target of approximately 40% of all modern medicinal drugs. Two of the United States's top five selling drugs (Hydrocodone and Lisinopril) act by targeting a G protein–coupled receptor. The 2012 Nobel Prize in Chemistry was awarded to Brian Kobilka and Robert Lefkowitz for their work that was ""crucial for understanding how G protein–coupled receptors function."". There have been at least seven other Nobel Prizes awarded for some aspect of G protein–mediated signaling.There are two principal signal transduction pathways involving the G protein–coupled receptors: the cAMP signal pathway and the phosphatidylinositol signal pathway. When a ligand binds to the GPCR it causes a conformational change in the GPCR, which allows it to act as a guanine nucleotide exchange factor (GEF). The GPCR can then activate an associated G protein by exchanging its bound GDP for a GTP. The G protein's α subunit, together with the bound GTP, can then dissociate from the β and γ subunits to further affect intracellular signaling proteins or target functional proteins directly depending on the α subunit type (Gαs, Gαi/o, Gαq/11, Gα12/13).