MECHANISM OF PROTEIN SYNTHESIS
The DNA code is a . Each triplet, a group of three bases, codes for a specific amino acid:
Fig. 8.16 Translation process of protein synthesis in prokaryotes.
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Fig. 2. Signal transduction in insulin action. The insulin receptor is a tyrosine kinase that undergoes autophosphorylation, and catalyses the phosphorylation of cellular proteins such as members of the IRS family, Shc, and Cbl. These pathways act in a concerted fashion to coordinate the regulation of vesicle trafficking, protein synthesis, enzyme activation and inactivation, and gene expression, which results in the regulation of glucose, lipid, and protein metabolism.
ENZYME FOR PROTEIN SYNTHESIS - Liberty Public Market
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USE of appendices in dissertation enzyme for protein synthesis
i.ρ-dependent Termination: In some prokaryotes, the termination of transcription is helped by a ρ (rho) protein that gets attached at the 5′ end of the newly synthesizing mRNA. The ρ then moves along the mRNA and induces the formation of hairpin loop near the 3′ end of mRNA due to the presence of inverted repeated sequences. This helps in the detachment of mRNA from the DNA (Fig. 8.9).
The process of synthesis of proteins from mRNA (translation of language of nucleic acids into the language of proteins) is called translation. There are 20 different types of amino acids, which constitute various proteins, and these amino acids themselves cannot recognize their respective codons in the mRNA. Different amino acids are carried by their specific tRNA molecules at the
site of protein synthesis (mRNA). There are about 55 types of tRNA molecules available in the cytoplasm, so that one amino acid may have more than one tRNAs.
The Role of DNA in Protein and Enzyme Synthesis
Protein Synthesis - Department of Chemistry
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MECHANISM OF PROTEIN SYNTHESIS | Biology …
MECHANISM OF PROTEIN SYNTHESIS
Hyperlipidemia is one of the features of obesity induced T2DM. When circulating NEFAs are greater than the oxidative capacity of the heart, NEFAs are stored as intramyocardial triglycerides. Both NEFAs and TG contribute to cardiac lipotoxicity and worsened heart failure (27-32). High levels of circulating NEFAs promote insulin resistance by impairment of insulin-Akt activation and compensatory hyperinsulinemia (27, 33-36). NEFAs also induce the activation of atypical protein kinase C (PKC)0, which is a serine/threonine kinase that phosphorylates and subsequently activates IkB kinase. Then IkB kinase phosphorylates insulin receptor substrate-1 (IRS-1) serine residues which inhibit the ability of IRS-1 to bind to SH2 domains of the p85 regulatory subunit of phosphatidylinositol 3-kinase (PI3K), and consequently impair insulin signal transduction (36). NEFAs not only trigger the development of cardiac insulin resistance but also lead to the development of myocardial contractile dysfunction. NEFAs can directly alter myocardial contractility by increasing NEFA flux into the myocardium. A recent study suggests that increasing the entry of fatty acyl coenzyme A (CoA) into the cardiomyocytes may modulate the Katp channel opening during the contractile state of the myocardium (37). Activation of KATP channel contributes to shortening of the action potential and decreases trans-sarcolemmal calcium flux and subsequent myocardial contractility (37).
Complete Information on Mechanism of Protein Synthesis …
Enzymes that work together to regulate the same set of chemical reactions group together
to form enzyme complexes (which may be transient) which are nano-machines with intricate and minute moving mechanical and
One example is the
Enzyme patterns and protein synthesis during …
Under normal physiological conditions, the main role of insulin on the heart is the regulation of substrate utilization. Insulin regulates cardiac metabolism by modulating glucose and fatty acid transport, glycolysis, glycogen synthesis, lipid metabolism, protein synthesis, growth, contractility, and apoptosis in the cardiomyocytes (5). The actions of insulin are mediated by binding to specific cell surface receptors (insulin receptor, InsR). Each cardiomyocyte is expressed at levels of about 10,000 to 100,000 receptors of InsR. The InsR is a tetrameric enzyme comprising two extracellular a-subunits and two transmembrane P-subunits (5). The binding of insulin to the extracellular domain of InsR triggers the activation of intrinsic tyrosine kinase activity of the P-subunits of the receptor. This leads to an autotransphosphorylation of the receptor where one P-subunit phosphorylates the other on several tyrosine residues. Once activated and phosphorylated, InsR binds via its phosphotyrosine residues and phosphorylates a series of downstream elements, including the insulin receptor substrate (IRS) family and Shc (5, 50). This recruitment and activation lead to the activation of two main pathways, the phosphatidylinositol 3-kinase (PI3K) and the mitogen-activated protein kinase (MAPK) pathway respectively. PI3K is considered to be the main player of the metabolic action of insulin, whereas the MAPK pathway is principally involved in cell growth and differentiation in the heart (Fig.2) (50, 51).
Mechanisms of Protein Synthesis by the Ribosome
9. As the ribosome moves by two codons, next round of protein synthesis is initiated by the attachment of a new ribosome. Thus, at a time, a single mRNA is found to be attached with many ribosomes with their polypeptides of different length, (shortest polypeptide at the 5′ end of the mRNA and longest at the 3′ end), called polysomes.
Fig. 8.15 Peptide bond formation in growing polypeptide.
10. Ultimately, the A-site of ribosome is occupied by the termination codon (UAA,UAG or UGA) at the 3′ end of mRNA, which is not recognized by any tRNA. Thus, the termination of the protein synthesis is helped by the release factors RFl, RF2 and RF3 (in eukaryotes eRF1), which release the newly synthesized polypeptide chain from the P-site (Fig. 8.16).
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