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Science 2 November 1990:
Vol. 250. no. 4981, pp. 646 - 651
DOI: 10.1126/science.2237415

Articles

Science, Vol 250, Issue 4981, 646-651
Copyright © 1990 by American Association for the Advancement of Science


articles

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

KT O'Neil and WF DeGrado

Central Research and Development Department, E. I. du Pont de Nemours and Company, Wilmington, DE 19880-0328.

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 that is surrounded by small, neutral amino acid side chains. Each of the commonly occurring amino acids was substituted into this guest site, and the resulting equilibrium constants for the monomer-dimer equilibrium were determined to provide a list of free energy difference (delta delta G degree) values.


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Science 262, 1680-1685
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A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants.
P. Harbury, T Zhang, P. Kim, and T Alber (1993)
Science 262, 1401-1407
   Abstract »    PDF »
Structure at 2.5 A of a designed peptide that maintains solubility of membrane proteins.
C. Schafmeister, L. Miercke, and R. Stroud (1993)
Science 262, 734-738
   Abstract »    PDF »
Structural basis of amino acid alpha helix propensity.
M Blaber, X. Zhang, and B. Matthews (1993)
Science 260, 1637-1640
   Abstract »    PDF »
JunB differs from c-Jun in its DNA-binding and dimerization domains, and represses c-Jun by formation of inactive heterodimers..
T Deng and M Karin (1993)
Genes & Dev. 7, 479-490
   Abstract »    PDF »
Crystal structure of a synthetic triple-stranded alpha-helical bundle.
B Lovejoy, S Choe, D Cascio, D. McRorie, W. DeGrado, and D Eisenberg (1993)
Science 259, 1288-1293
   Abstract »    PDF »
Role of transmembrane domain interactions in the assembly of class II MHC molecules.
P Cosson and J. Bonifacino (1992)
Science 258, 659-662
   Abstract »    PDF »
Internal stark effect measurement of the electric field at the amino terminus of an alpha helix.
D. Lockhart and P. Kim (1992)
Science 257, 947-951
   Abstract »    PDF »
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.
E. O'Shea, J. Klemm, P. Kim, and T Alber (1991)
Science 254, 539-544
   Abstract »    PDF »
An Intrahelical Salt Bridge within the Trigger Site Stabilizes the GCN4 Leucine Zipper.
R. A. Kammerer, V. A. Jaravine, S. Frank, T. Schulthess, R. Landwehr, A. Lustig, C. Garcia-Echeverria, A. T. Alexandrescu, J. Engel, and M. O. Steinmetz (2001)
J. Biol. Chem. 276, 13685-13688
   Abstract »    Full Text »    PDF »



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