Search results
Results From The WOW.Com Content Network
Glycine is integral to the formation of alpha-helices in secondary protein structure due to the "flexibility" caused by such a small R group. Glycine is also an inhibitory neurotransmitter [ 9 ] – interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited ...
The glycine protein system is regenerated when the H-protein is oxidized to regenerate the disulfide bond in the active site by interaction with the L-protein, which reduces NAD + to NADH and H +. When coupled to serine hydroxymethyltransferase , the glycine cleavage system overall reaction becomes:
Glycine cleavage system H protein, mitochondrial (abbreviated as GCSH) is a protein that in humans is encoded by the GCSH gene. [4] [5] [6] Degradation of glycine is brought about by the glycine cleavage system (GCS), which is composed of 4 protein components: P protein (a pyridoxal phosphate-dependent glycine decarboxylase), H protein (a lipoic acid-containing protein; this protein), T ...
Taken together, these factors would suggest that the glycine of the original protein adopts α-helical structure, rather than random coil. Several types of methods are used to combine all the available data to form a 3-state prediction, including neural networks, hidden Markov models and support vector machines. Modern prediction methods also ...
The protein Gephyrin has been shown to be necessary for GlyR clustering at inhibitory synapses. [ 5 ] [ 6 ] GlyR is known to colocalize with the GABA A receptor on some hippocampal neurons . [ 5 ] Nevertheless, some exceptions can occur in the central nervous system where the GlyR α1 subunit and gephyrin, its anchoring protein, are not found ...
Co-translational addition of myristic acid by N-myristoyltransferase to N-terminal glycine of a nascent protein. Myristoylation is a lipidation modification where a myristoyl group , derived from myristic acid , is covalently attached by an amide bond to the alpha-amino group of an N -terminal glycine residue. [ 1 ]
Crystal structure of an extracellular segment of integrin alphaVbeta3 complexed with a cyclic peptide containing the arginyl-glycyl-aspartic acid (RGD) sequence. RGD is shown in maroon. CEND-1, also known as iRGD, is a cyclic peptide that homes to tumors via binding to integrin alpha V receptors. [22]
Very abundant and very versatile, it is more stiff than glycine, but small enough to pose only small steric limits for the protein conformation. It behaves fairly neutrally, and can be located in both hydrophilic regions on the protein outside and the hydrophobic areas inside. Asparagine or aspartic acid: B Asx