Surface and inside volumes in globular proteins

@article{Janin1979SurfaceAI,
  title={Surface and inside volumes in globular proteins},
  author={Jo{\"e}l Janin},
  journal={Nature},
  year={1979},
  volume={277},
  pages={491-492}
}
  • J. Janin
  • Published 8 February 1979
  • Chemistry, Biology
  • Nature
MEASUREMENTS of the surface area accessible to solvent provide a convenient definition of the surface and the inside volumes in proteins of known X-ray structure. The study of the accessibility to solvent of amino acid residues in several proteins1–3 has confirmed the early observation that polar residues are found mostly on the surface and non-polar residues mostly inside globular protein structures. But the accessibility shows systematic variations with the molecular weight, because of the… 

Interior and surface of monomeric proteins.

Amino acid hydrophobicity and accessible surface area.

The present findings indicate that the variation of the accessible surface area describes an alternative hydrophobicity scale.

Distribution of accessible surfaces of amino acids in globular proteins

This report shows that a complete description of accessible surface areas is given by parametric distribution fuctions with three modes; the modes are formed by partitioning the available accessible surface area of the amino acids into three segments; the data for each segment are characterized by a mode‐specific model.

Protein engineering the surface of enzymes.

The multilayered organization of water-soluble proteins

An analysis of both the surfaces and the interiors of a set of water-soluble monomeric proteins in terms of solvent-excluded surface (SES) and atomic partial charge shows that the surface of a soluble monomer has a net negative charge and is much smoother than the interior.

Prediction of the surface-interior diagram of globular proteins by an empirical method.

  • K. NishikawaT. Ooi
  • Computer Science
    International journal of peptide and protein research
  • 1980
The results show that an adequate smoothing of a parameter set is the best way to reduce the extent of biasing towards the data base and to give the best prediction for 'unknown' proteins.

Geometric structural aspects of proteins and newcomb-benford law

The present findings indicate that the hydrophobic effect is responsible for the anomalous first digit behavior of solvent-accessible surface areas.
...

References

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An analysis of 15 protein structures indicates: First, the loss of accessible surface area by monomeric proteins on folding—proportional to hydrophobic energy—is a simple function of molecular

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