Glycine is an amino acid that has a single hydrogen atom as its side chain.
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Glycine is an amino acid that has a single hydrogen atom as its side chain.
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Glycine is integral to the formation of alpha-helices in secondary protein structure due to its compact form.
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Glycine is an inhibitory neurotransmitter – interference with its release within the spinal cord can cause spastic paralysis due to uninhibited muscle contraction.
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Glycine was discovered in 1820 by the French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid.
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Glycine originally called it "sugar of gelatin", but the French chemist Jean-Baptiste Boussingault showed that it contained nitrogen.
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Glycine is cogenerated as an impurity in the synthesis of EDTA, arising from reactions of the ammonia coproduct.
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Glycine is not essential to the human diet, as it is biosynthesized in the body from the amino acid serine, which is in turn derived from 3-phosphoglycerate, but the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen synthesis.
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Glycine is extremely sensitive to antibiotics which target folate, and blood glycine levels drop severely within a minute of antibiotic injections.
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Glycine is an inhibitory neurotransmitter in the central nervous system, especially in the spinal cord, brainstem, and retina.
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Glycine is a required co-agonist along with glutamate for NMDA receptors.
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Glycine is not widely used in foods for its nutritional value, except in infusions.
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Glycine is an intermediate in the synthesis of a variety of chemical products.
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Glycine is a significant component of some solutions used in the SDS-PAGE method of protein analysis.
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Glycine is used to remove protein-labeling antibodies from Western blot membranes to enable the probing of numerous proteins of interest from SDS-PAGE gel.
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Glycine had previously been identified in the Murchison meteorite in 1970.
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