Structural studies on the ras-gene-encoded oncogenic p21 proteins

Matthew R. Pincus

Research output: Contribution to journalConference articlepeer-review


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 languageEnglish
Pages (from-to)213
Number of pages1
JournalAmerican Chemical Society, Polymer Preprints, Division of Polymer Chemistry
Issue number1
StatePublished - Apr 1990
Externally publishedYes
EventPapers Presented at the Boston, Massachusetts Meeting of ACS 1989 - Boston, MA, USA
Duration: 22 Apr 198927 Apr 1989


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