Prediction of Secondary Structure in Proteins

The numbers in parentheses are degrees of polymerization. The b0 values in the case of addition of salts to poly(a,y-dia-minobutyric acid) solution at pH are indicated. , 2.0 M KSCN V, 2.0 M KC1 

Conformation boundary residues are numbered as well as the six proline residues represented by O 

For the past few years, complete amino acid sequences have been determined from the nucleotide sequences of structural genes. 

The knowledge of amino acid sequences of proteins may provide their three-dimensional structures if CD predictions are valid. However, the CD prediction for the secondary structure of a given protein, especially having (3-sheet structures, is not valid enough to probe the structure-function relationships in native proteins. We are awaiting the development of a more precise prediction method for secondary structures of proteins. 

Membrane-bound proteins extend from the cytoplasmic membrane. Analysis by the method of Kyte and Doolittle 186 is quite useful for predicting the protein segments extending into the cytoplasmic membrane. The Kyte and Doolittle method, the so-called hydropathic index method, if it is coupled with the Chou-Fasman method, safely differentiates the protein segment which is located outside the membrane, from the helices within the membrane. The best examples are cytochrome P-450 187), cytochrome b5188), reaction centers 189,190) and light-harvesting protein comple- 

---