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Myoglobin contains 154 amino acids. [35] Myoglobin contains a porphyrin ring with an iron at its center. A proximal histidine group (His-93) is attached directly to iron, and a distal histidine group (His-64) hovers near the opposite face. [35] The distal imidazole is not bonded to the iron, but is available to interact with the substrate O 2.
During translation, amino acids are joined into a linear chain by condensation reactions which create peptide bonds between the carboxyl group of one amino acid and the amino group of an adjacent amino acid. The first and last amino acids in the chain are said to be N-terminal and C-terminal, respectively, in reference to the unbonded amino ...
The polar, uncharged amino acids serine (Ser, S), threonine (Thr, T), asparagine (Asn, N) and glutamine (Gln, Q) readily form hydrogen bonds with water and other amino acids. [32] They do not ionize in normal conditions, a prominent exception being the catalytic serine in serine proteases. This is an example of severe perturbation, and is not ...
Note, in the diagram, the presence of non-polar(gold) amino acids along one side of the helix when viewed through the longitudinal axis, as well as charged/polar amino acids along the other face. This provides this structure with longitudinal amphipathic properties necessary for hydrophobic aggregation along the non-polar side.
Otherwise, there will be a repulsive force pushing them apart. The active site usually contains non-polar amino acids, although sometimes polar amino acids may also occur. [2] The binding of substrate to the binding site requires at least three contact points in order to achieve stereo-, regio-, and enantioselectivity.
Also non-standard amino acid. Any amino acid , natural or artificial, that is not one of the 20 or 21 proteinogenic amino acids encoded by the standard genetic code . There are hundreds of such amino acids, many of which have biological functions and are specified by alternative codes or incorporated into proteins accidentally by errors in ...
Most lipids consist of a polar or hydrophilic head (typically glycerol) and one to three non polar or hydrophobic fatty acid tails, and therefore they are amphiphilic. Fatty acids consist of unbranched chains of carbon atoms that are connected by single bonds alone (saturated fatty acids) or by both single and double bonds (unsaturated fatty ...
When these alpha helices dimerize, the zipper is formed. The hydrophobic side of the helix forms a dimer with itself or another similar helix, burying the non-polar amino acids away from the solvent. The hydrophilic side of the helix interacts with the water in the solvent.