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- W2095450147 abstract "(1) Co-operation between a laboratory interested in developing the theory for protein secondary structure prediction methods and a laboratory interested in applying and comparing such methods has led to the development of a simple predictive algorithm. (2) Four-state predictions, in which each residue is unambiguously assigned one conformational state of α-helix, extended chain, reverse turn or coil, predict 49% of residue states correctly (in a sample of 26 proteins) when the overall helix and extended-chain content is not taken into account. (3) When the relative abundances of helix, extended chain, reverse turn and coil observed by X-ray crystallography are taken into account, a single constant for each protein and type of conformation can be used to bias the prediction. When predictions are optimized in this way, 63% of all residue states are unambiguously and correctly assigned. (4) By analysing the nature of the bias required, proteins can be classified into helix-rich types, pleated-sheet-rich types, and so on. It is shown that, if the type of protein can be determined even approximately by circular dichroism, 57% of residue states can be correctly predicted without taking into account the X-ray structure. Further, comparable predictions can be obtained if, instead of circular dichroism, preliminary predictions are made to assess the protein type. (5) It is emphasized that the numbers quoted here depend on the method used to assess accuracy, and the algorithm is shown to be at least as good as, and usually superior to, the reported prediction methods assessed in the same way. (6) Ways of further enhancing predictions by the use of additional information from hydrophobic triplets and homologous sequences are also explored. Hydro-phobic triplet information does not significantly improve predictive power and it is concluded that this information is used by proteins in the next stage of folding. On the other hand, the use of homologous sequences appears to be very promising. (7) The implication of these results in protein folding is discussed." @default.
- W2095450147 created "2016-06-24" @default.
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- W2095450147 date "1978-03-01" @default.
- W2095450147 modified "2023-10-14" @default.
- W2095450147 title "Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins" @default.
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- W2095450147 doi "https://doi.org/10.1016/0022-2836(78)90297-8" @default.
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