Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence

Protein Eng. 1990 Dec;4(2):155-61. doi: 10.1093/protein/4.2.155.


Statistical analysis of 12 unstable and 32 stable proteins revealed that there are certain dipeptides, the occurrence of which is significantly different in the unstable proteins compared with those in the stable ones. Based on the impact of these dipeptides on the unstable proteins over the stable ones, a weight value of instability is assigned to each of the dipeptides. For a given protein the summation of these weight values normalized to the length of its sequence helps to distinguish between unstable and stable proteins. Results suggest that the in vivo instability of proteins is possibly determined by the order of certain amino acids in its sequence. An attempt is made to correlate metabolic stability of proteins with features of their primary sequence where weight values of instability for a protein of known sequence could thus be used as an index for predicting its stability characteristics.

MeSH terms

  • Amino Acid Sequence
  • Dipeptides / chemistry*
  • Enzyme Stability
  • Enzymes / chemistry*
  • Half-Life
  • Proteins / chemistry*


  • Dipeptides
  • Enzymes
  • Proteins