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In analogous experiments with other synthetic RNAs, they found that poly-C directed synthesis of polyproline. Nirenberg recounts that the labs of Severo Ochoa and James Watson had earlier done similar experiments with poly-A, but failed to detect protein synthesis because polylysine (unlike most proteins) is soluble in trichloroacetic acid.
Alexander Latham Dounce (December 7, 1909 – April 24, 1997) was an American professor of biochemistry. Among his fields of study were the isolation and purification of cellular organelles, protein crystallization, enzymes (specifically catalase), DNA binding proteins, and the chemical basis of protein synthesis.
Regulation of protein synthesis is partly influenced by phosphorylation of eIF2 (via the α subunit), which is a part of the eIF2-GTP-Met-tRNA i Met ternary complex (eIF2-TC). When large numbers of eIF2 are phosphorylated, protein synthesis is inhibited. This occurs under amino acid starvation or after viral infection.
Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino ...
Once the initiation factor helps the tRNA bind, the GTP hydrolyzes and is released the eIF2. The eIF2 beta subunit is identified by its Zn-finger. The eIF2 alpha subunit is characterized by an OB-fold domain and two beta strands. This subunit helps to regulate translation, as it becomes phosphorylated to inhibit protein synthesis. [2]
The synthetase first binds ATP and the corresponding amino acid (or its precursor) to form an aminoacyl-adenylate, releasing inorganic pyrophosphate (PPi).The adenylate-aaRS complex then binds the appropriate tRNA molecule's D arm, and the amino acid is transferred from the aa-AMP to either the 2'- or the 3'-OH of the last tRNA nucleotide (A76) at the 3'-end.
Phosphorylation of selected tyrosine sites on receptor substrates is known to activate different pathways leading to increased glucose uptake, lipogenesis, and glycogen and protein synthesis, as well as to the stimulation of cell growth. In addition to the activation of these pathways by tyrosine phosphorylation, several mechanisms of ...
Translation initiation is the most highly regulated step of protein synthesis in prokaryotes. [5] The rate of translation depends on two factors: the rate at which a ribosome is recruited to the RBS; the rate at which a recruited ribosome is able to initiate translation (i.e. the translation initiation efficiency)