Hydrophobicity of Amino Acid Residues in Globular Proteins

American Association for the Advancement of Science (AAAS) - Tập 229 Số 4716 - Trang 834-838 - 1985
George D. Rose1, Ari Geselowitz1, Glenn J. Lesser1, Richard Lee1, Micheal H. Zehfus1
1Department of Biological Chemistry, The Milton S. Hershey Medical Center, The Pennsylvania State University, Hershey 17033

Tóm tắt

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 residues as either "exposed" or "buried." In the experiment reported in this article proteins of known structure were used to measure the average area that each residue buries upon folding. This characteristic quantity, the average area buried, is correlated with residue hydrophobicity.

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Tài liệu tham khảo

BERNSTEIN, F.C., PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES, JOURNAL OF MOLECULAR BIOLOGY 112: 535 (1977).

CHOTHIA, C, PRINCIPLES THAT DETERMINE THE STRUCTURE OF PROTEINS, ANNUAL REVIEW OF BIOCHEMISTRY 53: 537 (1984).

CHOTHIA, C, NATURE OF ACCESSIBLE AND BURIED SURFACES IN PROTEINS, JOURNAL OF MOLECULAR BIOLOGY 105: 1 (1976).

CHOTHIA, C, HYDROPHOBIC BONDING AND ACCESSIBLE SURFACE-AREA IN PROTEINS, NATURE 248: 338 (1974).

CHOTHIA, C, STRUCTURAL INVARIANTS IN PROTEIN FOLDING, NATURE 254: 304 (1975).

Cohn E. J. Proteins Amino Acids and Peptides as Ions and Dipolar Ions (1943).

Creighton, T. E., Proteins: CH6 (1983).

Eisenberg, D., Proceedings of the National Academy of Sciences of the United States of America 81: 140 (1984).

GUY, H.R., AMINO-ACID SIDE-CHAIN PARTITION ENERGIES AND DISTRIBUTION OF RESIDUES IN SOLUBLE-PROTEINS, BIOPHYSICAL JOURNAL 47: 61 (1985).

Hopp, T. P., Proceedings of the National Academy of Sciences of the United States of America 78: 3824 (1981).

JANIN, J, SURFACE AND INSIDE VOLUMES IN GLOBULAR PROTEINS, NATURE 277: 491 (1979).

KAUZMANN, W, SOME FACTORS IN THE INTERPRETATION OF PROTEIN DENATURATION, ADVANCES IN PROTEIN CHEMISTRY 14: 1 (1959).

KRIGBAUM, W.R., LOCAL INTERACTIONS AS A STRUCTURE DETERMINANT FOR PROTEIN MOLECULES .2., BIOCHIMICA ET BIOPHYSICA ACTA 576: 204 (1979).

10.1016/0022-2836(82)90515-0

LEE, B, INTERPRETATION OF PROTEIN STRUCTURES - ESTIMATION OF STATIC ACCESSIBILITY, JOURNAL OF MOLECULAR BIOLOGY 55: 379 (1971).

LEVITT, M, SIMPLIFIED REPRESENTATION OF PROTEIN CONFORMATIONS FOR RAPID SIMULATION OF PROTEIN FOLDING, JOURNAL OF MOLECULAR BIOLOGY 104: 59 (1976).

MANAVALAN, P, HYDROPHOBIC CHARACTER OF AMINO-ACID RESIDUES IN GLOBULAR PROTEINS, NATURE 275: 673 (1978).

MCMEEKIN, T.L., Studies in the physical chemistry of amino acids, peptides and related substances. III. The solubility of derivatives of the amino acids in alcohol-water mixtures, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 57: 626 (1935).

MEIROVITCH, H, EMPIRICAL-STUDIES OF HYDROPHOBICITY .1. EFFECT OF PROTEIN SIZE ON THE HYDROPHOBIC BEHAVIOR OF AMINO-ACIDS, MACROMOLECULES 13: 1398 (1980).

MIYAZAWA, S, ESTIMATION OF EFFECTIVE INTERRESIDUE CONTACT ENERGIES FROM PROTEIN CRYSTAL-STRUCTURES - QUASI-CHEMICAL APPROXIMATION, MACROMOLECULES 18: 534 (1985).

NISHIKAWA, K, PREDICTION OF THE SURFACE-INTERIOR DIAGRAM OF GLOBULAR-PROTEINS BY AN EMPIRICAL-METHOD, INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH 16: 19 (1980).

NOVOTNY, J, A PROGRAM FOR PREDICTION OF PROTEIN SECONDARY STRUCTURE FROM NUCLEOTIDE-SEQUENCE DATA - APPLICATION TO HISTOCOMPATIBILITY ANTIGENS, NUCLEIC ACIDS RESEARCH 12: 243 (1984).

NOZAKI, Y, SOLUBILITY OF AMINO ACIDS AND 2 GLYCINE PEPTIDES IN AQUEOUS ETHANOL AND DIOXANE SOLUTIONS - ESTABLISHMENT OF A HYDROPHOBICITY SCALE, JOURNAL OF BIOLOGICAL CHEMISTRY 246: 2211 (1971).

10.1126/science.653353

RICHARDS, F.M., AREAS, VOLUMES, PACKING, AND PROTEIN-STRUCTURE, ANNUAL REVIEW OF BIOPHYSICS AND BIOENGINEERING 6: 151 (1977).

ROBSON, B, JOURNAL OF MOLECULAR BIOLOGY 132: 19 (1979).

ROSE, G.D., TURNS IN PEPTIDES AND PROTEINS, ADVANCES IN PROTEIN CHEMISTRY 37: 1 (1985).

ROSE, G.D., AUTOMATIC RECOGNITION OF DOMAINS IN GLOBULAR-PROTEINS, METHODS IN ENZYMOLOGY 115: 430 (1985).

ROSE, G.D., PREDICTION OF CHAIN TURNS IN GLOBULAR PROTEINS ON A HYDROPHOBIC BASIS, NATURE 272: 586 (1978).

Rose, G. D., Proceedings of the National Academy of Sciences of the United States of America 77: 4643 (1980).

SHRAKE, A, ENVIRONMENT AND EXPOSURE TO SOLVENT OF PROTEIN ATOMS - LYSOZYME AND INSULIN, JOURNAL OF MOLECULAR BIOLOGY 79: 351 (1973).

SWEET, R.M., CORRELATION OF SEQUENCE HYDROPHOBICITIES MEASURES SIMILARITY IN 3-DIMENSIONAL PROTEIN-STRUCTURE, JOURNAL OF MOLECULAR BIOLOGY 171: 479 (1983).

Tanford C. The Hydrophobic Effect (1980).

VONHEIJNE, G, TRANS-MEMBRANE TRANSLOCATION OF PROTEINS - DIRECT TRANSFER MODEL, EUROPEAN JOURNAL OF BIOCHEMISTRY 97: 175 (1979).

WERTZ, D.H., INFLUENCE OF WATER ON PROTEIN-STRUCTURE - ANALYSIS OF PREFERENCES OF AMINO-ACID RESIDUES FOR INSIDE OR OUTSIDE AND FOR SPECIFIC CONFORMATIONS IN A PROTEIN MOLECULE, MACROMOLECULES 11: 9 (1978).

WOLFENDEN, R, AFFINITIES OF AMINO-ACID SIDE-CHAINS FOR SOLVENT WATER, BIOCHEMISTRY 20: 849 (1981).

WOLFENDEN, R, WATERLOGGED MOLECULES, SCIENCE 222: 1087 (1983).

YUNGER, L.M., MEASUREMENT AND CORRELATION OF PARTITION-COEFFICIENTS OF POLAR AMINO-ACIDS, MOLECULAR PHARMACOLOGY 20: 602 (1981).

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American Association for the Advancement of Science (AAAS)

Tập 229 Số 4716

834-838

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