Abstract
Conformational analysis, based on the program ECEPP (Empirical Conformational Energies of Peptides Program), has been applied to determining the three-dimensional structures of two of the transforming regions of the GTP-binding p21 protein, viz, Tyr 4-Ala 18, herein called segment 1, and Ile 55-Met 67, herein called segment 2, including the effects of hydration. The author finds that segment 1 from the normal protein adopts a variety of conformations for residues 4-8 but adopts a bend with high probability at Ala 11-Gly 12 (CD* conformation) (6). It can also adopt a bend with lower probability (<5%) at Gly 12-Gly 13. Typical conformations are listed. Application of conformational energy calculations to segment 2 revealed that the segments from normal proteins adopt alpha-helices from Glu 62-Met 67 while oncogenic sequences either have this helix disrupted or have helix propagation from Gly 60-Met 67.
| Original language | English |
|---|---|
| Pages (from-to) | 213 |
| Number of pages | 1 |
| Journal | American Chemical Society, Polymer Preprints, Division of Polymer Chemistry |
| Volume | 31 |
| Issue number | 1 |
| State | Published - Apr 1990 |
| Externally published | Yes |
| Event | Papers Presented at the Boston, Massachusetts Meeting of ACS 1989 - Boston, MA, USA Duration: 22 Apr 1989 → 27 Apr 1989 |