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The interpretation of protein structures: estimation of static accesibility. J. Mol. Biol. 55, 379-400

published: 19 Nov 2009 (6:04)
doi:10.1016/0022-2836(71)90324-X

B. Lee and F. M. Richards

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Conn., U.S.A. Received 14 September 1970. Available online 29 October 2004

Abstract

A program is described for drawing the van der Waal's surface of a protein molecule. An extension of the program permits the accessibility of atoms, or groups of atoms, to solvent or solute molecules of specified size to be quantitatively assessed. As defined in this study, the accessibility is proportional to surface area. The accessibility of all atoms in the twenty common amino acids in model tripeptides of the type Ala-X-Ala are given for defined conformation. The accessibilities are also given for all atoms in ribonuclease-S, lysozyme and myogoblin. Internal cavities are defined and discussed. Various summaries of these data are provided. Forty to fifty per cent of the surface area of each protein is occupied by non-polar atoms. The actual numerical results are sensitive to the values chosen for the van der Waal's radii of the various groups. Since there is uncertainty over the correct values for these radii, the derived numbers should only be used as a qualitative guide at this stage.

The average change in accessibility for the atoms of all three proteins in going from a hypothetical extended chain to the folded conformation of the native protein is about a factor of 3. This number applies to both polar (nitrogen and oxygen) and non-polar (carbon and sulfur) atoms considered separately. The larger non-polar amino acids tend to be more buried in the native form of all three proteins. However, for all classes and for residues within a given class the accessibility changes on folding tend to be highly variable.

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