A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids.

@article{ONeil1990ATS,
  title={A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids.},
  author={Karyn T O'Neil and William F. DeGrado},
  journal={Science},
  year={1990},
  volume={250 4981},
  pages={646-51}
}
Amino acids have distinct conformational preferences that influence the stabilities of protein secondary and tertiary structures. The relative thermodynamic stabilities of each of the 20 commonly occurring amino acids in the alpha-helical versus random coil states have been determined through the design of a peptide that forms a noncovalent alpha-helical dimer, which is in equilibrium with a randomly coiled monomeric state. The alpha helices in the dimer contain a single solvent-exposed site… CONTINUE READING
Highly Influential
This paper has highly influenced 10 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 204 extracted citations

Similar Papers

Loading similar papers…