What is the process of protein synthesis? | Yahoo Answers
When protein and glucose were combined, the peak response was similar to that of glucose alone.
and the textbook to create a simplified summary of protein synthesis
Gluconeogenesis also is increased, and hepatic extraction of alanine, a key amino acid gluconeogenic precursor, is accelerated.19 Excessive rates of hepatic glucose production, proteolysis, and amino acid oxidation in type 1 diabetes are all reduced by insulin administration,82 but proteolysis and amino acid oxidation are more resistant to the suppressive effects of insulin.83 Normalization of protein metabolic rates may, therefore, require long-term tight metabolic control.84 Today, with improved glycemic management in type 1 diabetes, a more normal protein synthesis, breakdown, and oxidation should occur.
In the study by Nuttall et al.,10 when protein and glucose were combined, the peak response was similar to the peak response of glucose alone.
15/01/2018 · Overview of Protein Expression ..
The majority of protein is digested, and the amino acids not used for gut fuel are metabolized in the intestinal mucosal cells and transported by the portal vein to the liver for protein synthesis or gluconeogenesis.12 In the liver, nonessential amino acids are largely deaminated, and the amino group (nitrogen) removed is converted into urea for excretion in the urine.13 It has been shown that in subjects without and with mild type 2 diabetes, ~5070% of a 50-g protein meal is accounted for over an 8-hour period by deamination in the liver and intestine and synthesis to urea.14 It has been assumed that the remaining carbon skeletons from the nonessential amino acids are available for glucose synthesis, which would then enter into the general circulation.
Fifteen subjects with diabetes and three control subjects were fed breakfasts of glucose or carbohydrate or protein foods calculated to yield equal amounts of glucose (2 g protein/kg compared to 1 g carbohydrate/kg).
Protein Synthesis -Translation and Regulation
Translating the code into an actual protein chain is complicated by the fact that individual amino acids won't interact with the messenger RNA chain. The amino acids have to be carried to the messenger RNA by another type of RNA known as transfer RNA - abbreviated to tRNA (as opposed to mRNA for messenger RNA).
All of this is controlled by a - a hugely complicated structure involving protein molecules and yet another form of RNA (ribosomal RNA or rRNA).
DNA and Protein Synthesis - BioTopics
There are plenty of ideas, but few clear facts
26 Feb 2017: ...the common ancestor ...did encode many of the protein domains of all three super-kingdoms.
RCSB Protein Data Bank - RCSB PDB
The researchers attributed the decrease in calories to the higher satiating effect of protein compared to carbohydrate.
Welcome A Structural View of Biology
26 May 2011: The common ancestor of life on Earth had more functional protein domains than the first cells!
What's New and Beneficial About Soybeans
At the next stage, RNA molecules began to synthesize proteins, first by developing RNA adaptor molecules that can bind activated amino acids and then by arranging them according to an RNA template using other RNA molecules such as the RNA core of the ribosome.
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Eventually, the ribosome will come to a stop codon. The three stop codons don't code for any amino acids, and so the process comes to a halt. The protein chain produced up to that point is then released from the ribosome, and then folds itself up into its secondary and tertiary structures.
Low Protein Intake Is Associated with a ..
Major topics include General Techniques for Handling Nucleic Acids, DEP treatment of solutions, Phenol Extraction, Ethanol Precipitation of Nucleic Acids, PEG Precipitation of DNA, Restriction Enzyme Digestion, RNA mRNA extraction, RNA Slot Blots, Formaldehyde Denaturing Gels for RNA, Ribonuclease Protection Assay, Primer Extention, Riboprobe Synthesis , Subcloning of DNA fragments, and many more...
ER stress and the unfolded protein response - …
To understand the oxygen-binding properties of hemoglobin, wewill focus briefly on the structure of the protein and the metalcomplexes embedded in it.
Molecular biology protocols and methods ..
For example, Manfred Eigen of Germany's Max Planck Institute says, "There is no doubt that proteins, which are more easily formed, were first on the scene" .
Protein Controversies in Diabetes
The shape change in the heme group has important implicationsfor the rest of the hemoglobin protein, as well. When the ironatom moves into the porphyrin plane upon oxygenation, thehistidine residue to which the iron atom is attached is drawncloser to the heme group. This movement of the histidine residuethen shifts the position of other amino acids that are near thehistidine (Figure 6). When the amino acids in a protein areshifted in this manner (by the oxygenation of one of the hemegroups in the protein), the structure of the interfaces betweenthe four subunits is altered. Hence, when a single heme group inthe hemoglobin protein becomes oxygenated, the whole proteinchanges its shape. In the new shape, it is easier for the otherthree heme groups to become oxygenated. Thus, the binding of onemolecule of O2 to hemoglobin enhances the ability ofhemoglobin to bind more O2 molecules. This property ofhemoglobin is known as "cooperative binding."
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