The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns). The α-helix is the most abundant type of secondary structure in proteins. In these secondary structures, regular patterns of H-bonds are formed between the main chain NH and CO groups of spatially neighboring amino acids, and the amino acids have similar Φ and ψĪn alpha-helix with hydrogen bonds (yellow dots) The protein structure can be considered as a sequence of secondary structure elements, such as α helices and β sheets. Cysteine on the other hand can react with another cysteine residue to form one cystine and thereby form a cross link stabilizing the whole structure. Glycine takes on a special position, as it has the smallest side chain, only one hydrogen atom, and therefore can increase the local flexibility in the protein structure. These can be classified according to the chemistry of the side chain, which also plays an important structural role. Proteins consist mostly of 20 different types of L-α-amino acids (the proteinogenic amino acids). These groups can therefore interact in the protein structure. they have separated positive and negative charges (partial charges) in the carbonyl group, which can act as hydrogen bond acceptor and in the NH group, which can act as hydrogen bond donor. The peptide bonds in the chain are polar, i.e. This conformational flexibility is responsible for differences in the three-dimensional structure of proteins. Many conformations of this chain are possible due to the rotation of the main chain about the two torsion angles φ and ψ at the Cα atom (see figure). Proteins are chains of amino acids joined together by peptide bonds. A continuous evaluation of protein structure prediction web servers is performed by the community project CAMEO3D. Starting in 1994, the performance of current methods is assessed biannually in the CASP experiment (Critical Assessment of Techniques for Protein Structure Prediction). Protein structure prediction is one of the most important goals pursued by computational biology and it is important in medicine (for example, in drug design) and biotechnology (for example, in the design of novel enzymes). Structure prediction is different from the inverse problem of protein design. Protein structure prediction is the inference of the three-dimensional structure of a protein from its amino acid sequence-that is, the prediction of its secondary and tertiary structure from primary structure. Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure.
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