Proceedings of the National Academy

Brooks B and M Karplus 1983. Harmonic Dynamics of Proteins Normal Modes and Fluctuations in Bovine Pancreatic Trypsin Inhibitor. Proceedings of the National Academy of Sciences USA 80 6571-6575. 

M, A Wlodawer, L G Pedersen and T A Darden 1994. Atomic-level Accuracy in Simulations of irge Protein Crystals. Proceedings of the National Academy of Sciences USA 91 8715-8718. 

Bond C ], K-B Wong, ] Clarke, A R Ferscht and V Daggett 1997. Characterisation of Residual Structure in the Tliermally Denatured State of Barnase by Simulation and Experiment Description of the Folding Pathway. Proceedings of the National Academy of Sciences USA 94 13409-13413. 

Bryngelson J D and P G Wolynes 1987. Spin Glasses and the Statistical Mechanics of Protein Folding. Proceedings of the National Academy of Sciences LISA 84 7524-7528. 

Godzik A, J Skolnick and A Kolinski 1992. Simulations of the Folding Pathway of Triose Phosj Lsomerase-type a// Barrel Proteins. Proceedings of the National Academy of Sciences USA 89 1 2633. 

Pauling L, R B Corey and H R Bronson 1951. The Structure of Proteins Two Hydrogen-bonded He Configurations of the Polypeptide Chain. Proceedings of the National Academy of Sciences USA y . 211... 

Miyamoto S and P A Kollman 1993b. What Determines the Strength of Noncovalent Association of Ligands to Proteins in Aqueous Solution Proceedings of the National Academy of Sciences USA 90 8402-8406. 

Finnt, D. F., et al., 1987. Tandem qnadrnpole Fourier tran.sform ma.ss. spectrometry of oligopeptides and small protein.s. Proceedings of the National Academy of Sciences, U.S.A. 84 620—623. 

Klotz, I. M., 1996. Equilibrium constants and free energies in unfolding of proteins in urea solutions. Proceedings of the National Academy of Sciences 93 14411-14415. 

Xiong, H., Bnckwalter, B., Shieh, H.-M., and Hecht, M. H., 1995. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proceedings of the National Academy of Sciences 92 6349—6353. 

Chien, C.-X, et al., 1991. The two-hybrid system A method to identify and clone genes for proteins that interact with a protein of interest. Proceedings of the National Academy of Sciences U.S.A. 88 9578 — 9582. 

Cohen, S. N., Chang, A. C. Y, Boyer, H. W., and Helling, R. B., 1973. Construction of biologically functional bacterial plasmids in vitro. Proceedings of the National Academy of Sciences U.S.A. 70 3240 — 3244. The classic paper on the construction of chimeric plasmids. 

Grunstein, M., and Hogness, D. S., 1975. Colony hybridization A specific method for the isolation of cloned DNAs tliat contain a specific gene. Proceedings of the National Academy of Sciences U.S.A. 72 3961—3965. Article describing die colony hybridization technique for specific gene isolation. 

Palese, P, and Roizman, B., 1996. Genetic engineering of viruses and of virus vectors A preface. Proceedings of the National Academy of Sciences U.S.A. 93 11287-11425. A preface to a. series of papers from a colloquium on genetic engineering and mediods in gene dierapy. 

Young, R. A., and Davis, R. W., 1983. Efficient isolation of genes using and-body probes. Proceedings of the National Academy of Sciences U.S.A. 80 1194-1198. Using andbodies to screen protein expression libraries to isolate the structural gene for a specific protein. 

Garrett, R. M., et al., 1998. Human snlfite oxidase R160Q Identification of the mutation in a snlfite oxidase-deficient patient and expression and characterization of the mutant enzyme. Proceedings of the National Academy of Sciences HSA 95 6394—6398. 

Jagendorf, A. T, and Uribe, E., 1966. ATP formadon caused by acid-base transidon of spinach chloroplasts. Proceedings of the National Academy of Sciences, USA 55 170-177. The classic paper providing the first experimental verificadon of Mitchell s chemiosmodc hypodiesis. 

Adapted from Van Schaftingcn, E., and Hers, H.-G., 1981. Inhibition of frnctosc-1,6-bisphosphatasc by fructosc-2,6-bis-phosphatc. Proceedings of the National Academy of Science, USA 78 2861-2863.)... 

FIGURE 24.13 The subunit structure of medium chain acyl-CoA dehydrogenase from pig liver mitochondria. Note the location of the bound FAD (red). (Adapted from Kim, J-T., and Wiz, J., 1988. Structure of the medium-chain acyl-CoA clchyclro-genase from pig liver mitochonciria at 3-A resolution. Proceedings of the National Academy of Sciences, USA 85 6671-668. )... 

Sinanoglu, 0. [1961] Many-Electron Theory of Atoms and Molecules, Proceedings of the National Academy of Sciences of the United States of America, 47(8), p. 1217. 

For Further Reading D. Harman, The aging process, Proceedings of the National Academy of Sciences, 78 (2004), 7124. C. Goldberg, The quest for immortality Science at the frontiers of aging, Science News, 162 (August 31, 2002), 143. 

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