
Nature Rev.Mol.Cell Biol. 16
... H3K56ac has a higher affinity for histone chaperones and promotes chromatin assembly H3K56ac is positioned at the entry-exit points on nucleosomes and enhances unwrapping of DNA ...
... H3K56ac has a higher affinity for histone chaperones and promotes chromatin assembly H3K56ac is positioned at the entry-exit points on nucleosomes and enhances unwrapping of DNA ...
Journal of Bacteriology
... protein is exposed to the periplasmic side of the outer membrane and thus that the amino terminus of the PhoE protein part of the hybrid molecule faces the periplasm. However, an alternative possibility should be considered, i.e., the first residue of the PhoE protein part could be on the outside su ...
... protein is exposed to the periplasmic side of the outer membrane and thus that the amino terminus of the PhoE protein part of the hybrid molecule faces the periplasm. However, an alternative possibility should be considered, i.e., the first residue of the PhoE protein part could be on the outside su ...
Folie 1 - uni
... protein is cytosolic or membrane-bound – modifications like phosphorylation are part of common mechanisms for controlling the behavior of a protein, for instance, activating or inactivating an enzyme. ...
... protein is cytosolic or membrane-bound – modifications like phosphorylation are part of common mechanisms for controlling the behavior of a protein, for instance, activating or inactivating an enzyme. ...
Adding Protein Context to the Human Protein-Protein
... Interactions of proteins regulate signaling, catalysis, gene expression and many other cellular functions. Therefore, characterizing the entire human interactome is a key effort in current proteomics research. This challenge is complicated by the dynamic nature of protein-protein interactions (PPIs) ...
... Interactions of proteins regulate signaling, catalysis, gene expression and many other cellular functions. Therefore, characterizing the entire human interactome is a key effort in current proteomics research. This challenge is complicated by the dynamic nature of protein-protein interactions (PPIs) ...
harvesting chemical energy
... oxidized states as they accept and donate electrons. Each component of the chain becomes reduced when it accepts electrons from its “uphill” neighbor, which is less electronegative. It then returns to its oxidized form as it passes electrons to its more electronegative ...
... oxidized states as they accept and donate electrons. Each component of the chain becomes reduced when it accepts electrons from its “uphill” neighbor, which is less electronegative. It then returns to its oxidized form as it passes electrons to its more electronegative ...
Chapt 6
... • The NADH produced in glycolysis passes its electrons across the mitochondrial membrane to either NAD+ or FAD. Because FADH2 adds its electrons farther along the electron transport chain, it contributes less to the H+ gradient and thus generates less ATP. • Some of the energy of the H+ gradient may ...
... • The NADH produced in glycolysis passes its electrons across the mitochondrial membrane to either NAD+ or FAD. Because FADH2 adds its electrons farther along the electron transport chain, it contributes less to the H+ gradient and thus generates less ATP. • Some of the energy of the H+ gradient may ...
BIOLOGICAL SCIENCES - Plant Biology PP2A
... first receptor kinase to be assigned a role in root development (5), our knowledge about its signaling pathway in the root remains limited (15, 22). In addition to post-translational modifications such as phosphorylation, developmental programs and cellular functions largely rely on interactions bet ...
... first receptor kinase to be assigned a role in root development (5), our knowledge about its signaling pathway in the root remains limited (15, 22). In addition to post-translational modifications such as phosphorylation, developmental programs and cellular functions largely rely on interactions bet ...
Student Study Guide
... Glycolysis and the Krebs cycle supply electrons (via NADH) to the transport chain, which drives oxidative phosphorylation. Glycolysis occurs in the cytosol, the Krebs cycle in the mitochondrial matrix. The electron transport chain is built into the inner mitochondrial membrane. Web/CD Activity9B: Ov ...
... Glycolysis and the Krebs cycle supply electrons (via NADH) to the transport chain, which drives oxidative phosphorylation. Glycolysis occurs in the cytosol, the Krebs cycle in the mitochondrial matrix. The electron transport chain is built into the inner mitochondrial membrane. Web/CD Activity9B: Ov ...
chapter 9 cellular respiration: harvesting chemical
... Some ATP is also formed directly during glycolysis and the citric acid cycle by substrate-level phosphorylation. Here an enzyme transfers a phosphate group from an organic substrate to ADP, forming ATP. For each molecule of glucose degraded to carbon dioxide and water by respiration, the cell ...
... Some ATP is also formed directly during glycolysis and the citric acid cycle by substrate-level phosphorylation. Here an enzyme transfers a phosphate group from an organic substrate to ADP, forming ATP. For each molecule of glucose degraded to carbon dioxide and water by respiration, the cell ...
2. The citric acid cycle
... 3. Oxidative Phosphorylation • The process that generates most of the ATP is called oxidative phosphorylation because it is powered by redox reactions • A smaller amount of ATP is formed in glycolysis and the citric acid cycle by substrate-level phosphorylation • Oxidative phosphorylation accounts ...
... 3. Oxidative Phosphorylation • The process that generates most of the ATP is called oxidative phosphorylation because it is powered by redox reactions • A smaller amount of ATP is formed in glycolysis and the citric acid cycle by substrate-level phosphorylation • Oxidative phosphorylation accounts ...
Cellular Respiration and Photosynthesis
... *Glycolysis takes place in the cytoplasm. During glycolysis, 1 glucose molecule is broken down into 2 molecules of pyruvic acid. *4 ATP molecules are formed; however, glycolysis requires 2 ATP to break apart each molecule of glucose; therefore, the net energy produced during glycolysis is 2 ATP. * I ...
... *Glycolysis takes place in the cytoplasm. During glycolysis, 1 glucose molecule is broken down into 2 molecules of pyruvic acid. *4 ATP molecules are formed; however, glycolysis requires 2 ATP to break apart each molecule of glucose; therefore, the net energy produced during glycolysis is 2 ATP. * I ...
Quiz 2 Review Sheet
... 58. Know the functions of proteins. Know examples like hemoglobin, myosin, insulin, insulin receptor, ATP synthase, photosystem II, antibodies, HIV protease, etc… and under what category they would fall. 59. How small is a protein relative to the size of a cell? (use the analogy) How many hemoglobin ...
... 58. Know the functions of proteins. Know examples like hemoglobin, myosin, insulin, insulin receptor, ATP synthase, photosystem II, antibodies, HIV protease, etc… and under what category they would fall. 59. How small is a protein relative to the size of a cell? (use the analogy) How many hemoglobin ...
KATABOLISME KARBOHIDRAT
... established with few H+ in the matrix and many in the intermembrane space. The cristae also contain an ATP synthase complex through which hydrogen ions flow down their gradient from the intermembrane space into the matrix. The flow of three H+ through an ATP synthase complex causes a conformational ...
... established with few H+ in the matrix and many in the intermembrane space. The cristae also contain an ATP synthase complex through which hydrogen ions flow down their gradient from the intermembrane space into the matrix. The flow of three H+ through an ATP synthase complex causes a conformational ...
CHAPTER 9 CELLULAR RESPIRATION: HARVESTING CHEMICAL
... oxidized states as they accept and donate electrons. ° Each component of the chain becomes reduced when it accepts electrons from its “uphill” neighbor, which is less electronegative. ° It then returns to its oxidized form as it passes electrons to its more electronegative ...
... oxidized states as they accept and donate electrons. ° Each component of the chain becomes reduced when it accepts electrons from its “uphill” neighbor, which is less electronegative. ° It then returns to its oxidized form as it passes electrons to its more electronegative ...
Chapter 7 Body Systems
... • It breaks down chemical bonds in glucose molecules and releases about 5% of the energy stored in them • It prepares glucose for the second step in catabolism—the citric ...
... • It breaks down chemical bonds in glucose molecules and releases about 5% of the energy stored in them • It prepares glucose for the second step in catabolism—the citric ...
sv-lncs - Department of Computer Science and Engineering
... intricate arrangements that drive the proteins to fold and interact as they do. A single protein molecule can possess multiple domains causing difficulty in discovering a simple formula that dictates the manner by which protein interactions occur. There is no known way to identify a protein-protein ...
... intricate arrangements that drive the proteins to fold and interact as they do. A single protein molecule can possess multiple domains causing difficulty in discovering a simple formula that dictates the manner by which protein interactions occur. There is no known way to identify a protein-protein ...
CHAPTER 9 CELLULAR RESPIRATION: HARVESTING CHEMICAL
... oxidized states as they accept and donate electrons. Each component of the chain becomes reduced when it accepts electrons from its “uphill” neighbor, which is less electronegative. It then returns to its oxidized form as it passes electrons to its more electronegative ...
... oxidized states as they accept and donate electrons. Each component of the chain becomes reduced when it accepts electrons from its “uphill” neighbor, which is less electronegative. It then returns to its oxidized form as it passes electrons to its more electronegative ...
Cell Respiration
... reactions. Finally, in a series of reactions, each of the two three-carbon sugar phosphates is converted to pyruvate. In the process, an energyrich hydrogen is harvested as NADH, and two ATP molecules are formed. ...
... reactions. Finally, in a series of reactions, each of the two three-carbon sugar phosphates is converted to pyruvate. In the process, an energyrich hydrogen is harvested as NADH, and two ATP molecules are formed. ...
Introduction - MRC Laboratory of Molecular Biology
... from glycolytic flux • This provides a platform from which to further investigate whether the PPP and the related cellular redox state might play a more general role in cellular circadian timekeeping • That the systems of the PPP and ROS detoxification might be intrinsically linked with cellular tim ...
... from glycolytic flux • This provides a platform from which to further investigate whether the PPP and the related cellular redox state might play a more general role in cellular circadian timekeeping • That the systems of the PPP and ROS detoxification might be intrinsically linked with cellular tim ...
video slide - Wild about Bio
... NADH and FADH2 donate electrons to the electron transport chain Electrons drop in free energy as they go down the chain and are finally passed to O2, ...
... NADH and FADH2 donate electrons to the electron transport chain Electrons drop in free energy as they go down the chain and are finally passed to O2, ...
PINK1 positively regulates HDAC3 to suppress p53
... modulation of p53 function by HDAC3 remains unclear. Here, we show that cytoplasmic PTEN-induced putative kinase 1 (PINK1) directly binds to and phosphorylates HDAC3 at Ser-424 to enhance its histone deacetylase activity. We demonstrate that PINK1 prevents H2O2-induced C-terminal cleavage of HDAC3 b ...
... modulation of p53 function by HDAC3 remains unclear. Here, we show that cytoplasmic PTEN-induced putative kinase 1 (PINK1) directly binds to and phosphorylates HDAC3 at Ser-424 to enhance its histone deacetylase activity. We demonstrate that PINK1 prevents H2O2-induced C-terminal cleavage of HDAC3 b ...
Redox regulation of protein tyrosine phosphatases during receptor
... source of ROS in all cell types, 1– 5% of electrons from the respiratory chain being typically diverted to the formation of Oz2 2 by ubiquinone-dependent reduction [3] (Fig. 1a). Recent evidence supports the hypothesis that mitochondrial ROS production is not only related to apoptotic cell death [4] ...
... source of ROS in all cell types, 1– 5% of electrons from the respiratory chain being typically diverted to the formation of Oz2 2 by ubiquinone-dependent reduction [3] (Fig. 1a). Recent evidence supports the hypothesis that mitochondrial ROS production is not only related to apoptotic cell death [4] ...
video slide
... 4. The energy stored in a H+ gradient across a membrane couples the redox reactions of the electron transport chain to ATP synthesis 5. The H+ gradient is referred to as a protonmotive force a. emphasizing its capacity to do work b. the force drives H+ back across the membrane through H+ channels A ...
... 4. The energy stored in a H+ gradient across a membrane couples the redox reactions of the electron transport chain to ATP synthesis 5. The H+ gradient is referred to as a protonmotive force a. emphasizing its capacity to do work b. the force drives H+ back across the membrane through H+ channels A ...
The role of mutations in core protein of hepatitis B
... hepatocellular carcinoma [3]. The genome of hepatitis B virus encodes four overlapping open reading frames that are translated to viral core protein or HBc particle, the surface proteins, a reverse transcriptase (RT), and HBx [4]. The core protein is the major polypeptide of the nucleocapsid that du ...
... hepatocellular carcinoma [3]. The genome of hepatitis B virus encodes four overlapping open reading frames that are translated to viral core protein or HBc particle, the surface proteins, a reverse transcriptase (RT), and HBx [4]. The core protein is the major polypeptide of the nucleocapsid that du ...
Phosphorylation

Phosphorylation is the addition of a phosphate (PO43−) group to a protein or other organic molecule. Phosphorylation and its counterpart, dephosphorylation, turn many protein enzymes on and off, thereby altering their function and activity. Protein phosphorylation is one type of post-translational modification.Protein phosphorylation in particular plays a significant role in a wide range of cellular processes. Its prominent role in biochemistry is the subject of a very large body of research (as of March 2015, the Medline database returns over 240,000 articles on the subject, largely on protein phosphorylation).