Hydrophobicity of amino acid residues in globular proteins.

  title={Hydrophobicity of amino acid residues in globular proteins.},
  author={George D. Rose and A R Geselowitz and G J Lesser and R H Lee and Micheal H. Zehfus},
  volume={229 4716},
During biosynthesis, a globular protein folds into a tight particle with an interior core that is shielded from the surrounding solvent. The hydrophobic effect is thought to play a key role in mediating this process: nonpolar residues expelled from water engender a molecular interior where they can be buried. Paradoxically, results of earlier quantitative analyses have suggested that the tendency for nonpolar residues to be buried within proteins is weak. However, such analyses merely classify… 
Solvent accessible surface of globular proteins: how exposed and buried amino acid residues are divided
Introduction Globular protein structures are often divided into two regions, the surface, which is in contact with the surrounding molecules, and the interior, which is not accessible to the external
Hydrophobicity of amino acid subgroups in proteins
The mean area buried upon folding for every chemical group in each residue within a set of X‐ray elucidated proteins is calculated and it is observed that, on average, each type of group buries a constant fraction of its standard state area.
Hydrophobic organization of membrane proteins.
A method of sequence analysis is described, based on the periodicity of residue replacement in homologous sequences, that extends conclusions derived from the known atomic structure of the reaction center to the more extensive database of putative transmembrane helical sequences.
Distinct Molecular Surfaces and Hydrophobicity of Amino Acid Residues in Proteins
  • L. Pacios
  • Chemistry, Biology
    J. Chem. Inf. Comput. Sci.
  • 2001
Hydrophobicity is a useful concept to rationalize the role played by amino acid residues in terms of buried or exposed conformation with regard to the aqueous environment in proteins. The
Hydrophobic distribution and spatial arrangement of amino acid residues in membrane proteins.
The hydrophobic variation of amino acid residues at various ranges in membrane and aqueous parts of membrane proteins is analysed to understand their structure and stability.
Hydrophobic Amino Acid Composition Patterns over Secondary Structure Elements of Proteins
This paper experimentally shows that the hydrophobic residues collectively reveal different composition patterns over different secondary structure elements, and quantitatively compares them using the statistical moments.
Prediction and Analysis of Surface Hydrophobic Residues in Tertiary Structure of Proteins
The ability to predict surface accessibility of hydrophobic residues directly from the sequence is of great help in choosing the sites of chemical modification or specific mutations and in the studies of protein stability and molecular interactions.
Stabilization Energies of Protein Conformation
The study of protein stability is currently undergoing a dramatic change. Early work, especially after Kauzmann (1959), centered on the analysis of simple chemical model systems to determine the
Prediction of transmembrane helices from hydrophobic characteristics of proteins.
A surrounding hydrophobicity scale applicable to membrane proteins is developed and a predictive scheme based on this scale predicts from amino acid sequence, transmembrane segments in PRC and randomly selected 26 membrane proteins to 80% level of accuracy.


Hydrophobic character of amino acid residues in globular proteins
A better index of protein hydrophobicity is introduced, showing very good correlation with the extent to which residues are buried5 compared with the hydrophobic indices used previously, and it could be used to characterise tertiary structures.
Hydrophobic bonding and accessible surface area in proteins
THE hydrophobic bond is the term used by Kauzmann1 to describe the gain in free energy on the transfer of non-polar residues from an aqueous environment to the interior of proteins. This has been
The nature of the accessible and buried surfaces in proteins.
  • C. Chothia
  • Materials Science
    Journal of molecular biology
  • 1976
Structural invariants in protein folding
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
Surface and inside volumes in globular proteins
The study of the accessibility to solvent of amino acid residues in several proteins 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.
Influence of water on protein structure. An analysis of the preferences of amino acid residues for the inside or outside and for specific conformations in a protein molecule.
There are generally significant changes in the conformational preferences of the residues in going from the inside to the outside of proteins; environmental (rather than local) solute-solvent interactions seem to be the predominant cause of these changes in conformational preference.
Automatic recognition of domains in globular proteins.
  • G. Rose
  • Biology
    Methods in enzymology
  • 1985