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 weight; second, the proportion of polar groups forming intramolecular hydrogen bonds is constant; and third, protein interiors are closely packed, each residue occupying the same volume as it does in crystals of amino acids.

[1]  R. Oppermann.  Proteins, amino acids and peptides , 1943 .

[2]  W. Kauzmann.  Some factors in the interpretation of protein denaturation. , 1959, Advances in protein chemistry.

[3]  C. Tanford.  Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of Proteins , 1962 .

[4]  I. M. Klotz,et al.  Hydrogen Bonds between Model Peptide Groups in Solution , 1962 .

[5]  D. Newth,et al.  Principles of Biomolecular Organization , 1967 .

[6]  Michel E. Goldberg,et al.  Tertiary structure of Escherichia coli β-d-galactosidase☆ , 1969 .

[7]  M. Levitt,et al.  Refinement of protein conformations using a macromolecular energy minimization procedure. , 1969, Journal of molecular biology.

[8]  J. L. Finney,et al.  Random packings and the structure of simple liquids. I. The geometry of random close packing , 1970, Proceedings of the Royal Society of London. A. Mathematical and Physical Sciences.

[9]  B. Lee,et al.  The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.

[10]  C. Tanford,et al.  The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. , 1971, The Journal of biological chemistry.

[11]  G N Cohen,et al.  The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. , 1972, European journal of biochemistry.

[12]  K. D. Watenpaugh,et al.  Refinement of the model of a protein: rubredoxin at 1.5 Å resolution , 1973 .

[13]  Hans Eklund,et al.  Structure of Liver Alcohol Dehydrogenase at 2.9-Å Resolution , 1973 .

[14]  L. H. Wright,et al.  Variability in the tertiary structure of alpha-chymotrypsin at 2.8-A resolution. , 1973, Biochemistry.

[15]  T. Steitz,et al.  Structure of yeast hexokinase. II. A 6 angstrom resolution electron density map showing molecular shape and heterologous interaction of subunits. , 1973, Journal of molecular biology.

[16]  A. Shrake,et al.  Environment and exposure to solvent of protein atoms. Lysozyme and insulin. , 1973, Journal of molecular biology.

[17]  F. Richards.  The interpretation of protein structures: total volume, group volume distributions and packing density. , 1974, Journal of molecular biology.

[18]  C. Chothia,et al.  Hydrophobic bonding and accessible surface area in proteins , 1974, Nature.

[19]  M. Levitt,et al.  Energy refinement of hen egg-white lysozyme. , 1974, Journal of molecular biology.