Protein folding implications

J Novotny, R Bruccoleri, M Karplus. An analysis of incorrectly folded protein models Implications for structural predictions. J Mol Biol 177 787-818, 1984. 

P Koehl, M Delame. Polar and nonpolar atomic environments m the protein core Implication for folding and binding. Pi-otems 20 264-278, 1994. 

Beckmann, R.P., Mizzen, L.A., Welch, W.J. (1990). Interaction of hsp70 with newly synthesized proteins Implications for protein folding and assembly. Science 248,2241-2249. 

Pappu, R. V., Srinivasan, R., and Rose, G. D. (2000). The Flory isolated-pair hypothesis is not valid for polypeptide chains Implications for protein folding. Proc. Natl. Acad. Sci. USA 97, 12565-12570. 

These moieties (particularly (5.95b)) are prominent in protein chemistry, and mechanisms for controlling their torsional stiffness have obvious potential implications for protein-folding processes. 

Eliezer D., Yao J., Dyson H. J. and Wright P. E. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat. Struct. Biol. (1998) 5(2) 148-155. 

In contrast, we also know of a great many cases in which a very small change in primary structure has major implications for biological function sickle cell anemia is a prominent example to which I return shortly. So we have a question. How are we to know when a change in primary structure is likely to alter the three-dimensional structure and biological properties of a protein To get at that question, we need to understand more about why a protein folds up in the way that it does. 

E.S. Eberhardt, R.T. Raines, Amide-amide and amide-water hydrogen bonds Implications for protein folding and stability, J. Am. Chem. Soc. 116 (1994) 2149-2150. 

Knhlman, B., J.A. Boice, W.J. Wn, R. Fairman, and D.P. Raleigh, Calcium binding peptides from alpha-lactalbumin implications for protein folding and stability. Biochemistry, 1997.36(15) 4607-15. 

Among cysteine proteases of bacteria is a papainlike enzyme from Clostridium histolyticum with a specificity similar to that of trypsin 338 Tire anaerobic Porphyromonas gingivalis, which is implicated in perio-dental disease, produces both arginine- and lysine-specific cysteine proteases designated gingipains.339 3393 Some virally encoded cysteine proteases, including one from the polio virus, have trypsin-like sequences with the serine of the catalytic triad replaced by cysteine.340 341 A human adenovirus protease also has a Cys His Glu triad but a totally different protein fold.342... 

Kim, E. I., Paliwal, S., Wilcox, C. S., Measurements of molecular electrostatic field effects in edge- to-face aromatic interactions and CH-p interactions with implications for protein folding and molecular recognition. J. Am. Chem. Soc. 

The great interest in this coil - to - globule transition is not only due to its importance as a general and fundamental concept in polymer physics and solution dynamics but also due to its deep implications in many biological systems, such as protein folding [71] and DNA packing [72],... 

B.1 Proline syn—anti Isomerization, Implications for Protein Folding... 

Heinemann, U., and Hahn, M. (1995). Circular permutation of polypeptide chains implications for protein folding and stability. Prog. Biophys. Mol. Biol, 64, 121-143. 

Scheiner S, Kar T (2005) Effect of solvent upon CH- O hydrogen bonds with implications for protein folding. J Phys Chem B 109 3681-3689... 

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