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Compaction and folding in model proteins

dc.contributor.authorChiu, Ting-Lanen_US
dc.contributor.authorGoldstein, Richard A.en_US
dc.date.accessioned2010-05-06T21:46:29Z
dc.date.available2010-05-06T21:46:29Z
dc.date.issued1997-09-15en_US
dc.identifier.citationChiu, Ting-Lan; Goldstein, Richard A. (1997). "Compaction and folding in model proteins." The Journal of Chemical Physics 107(11): 4408-4415. <http://hdl.handle.net/2027.42/70191>en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/70191
dc.description.abstractProtein folding is modeled as diffusion on a free-energy landscape, allowing use of the diffusion equation to study the impact of energetic parameters on the folding dynamics. The free-energy landscape is characterized by two different order parameters, one representing the degree of compactness, the other a measure of the progress towards the folded state. For marginally stable proteins, fastest folding is achieved when the nonspecific interactions favoring compaction are strong, resulting in a high folding temperature. Such proteins fold by rapid collapse followed by slower accumulation of correct contacts. © 1997 American Institute of Physics.en_US
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dc.format.extent156778 bytes
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dc.publisherThe American Institute of Physicsen_US
dc.rights© The American Institute of Physicsen_US
dc.titleCompaction and folding in model proteinsen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelPhysicsen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055en_US
dc.contributor.affiliationumDepartment of Chemistry and Biophysics Research Division, University of Michigan, Ann Arbor, Michigan 48109-1055en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/70191/2/JCPSA6-107-11-4408-1.pdf
dc.identifier.doi10.1063/1.474782en_US
dc.identifier.sourceThe Journal of Chemical Physicsen_US
dc.identifier.citedreferenceK. Kim and R. Baldwin, Annu. Rev. Biochem. 51, 459 (1982).en_US
dc.identifier.citedreferenceA. Šali, E. I. Shakhnovich, and M. J. Karplus, Nature (London) 369, 248 (1994).en_US
dc.identifier.citedreferenceK. A. Dill, Biochem. 24, 1501 (1985).en_US
dc.identifier.citedreferenceK. A. Dill, K. M. Fiebig, and H. S. Chan, Proc. Nat. Acad. Sci., U. S. A. 90, 1942 (1993).en_US
dc.identifier.citedreferenceN. Gō, Annu. Rev. Biophys. Bioeng. 12, 183 (1983).en_US
dc.identifier.citedreferenceM. Karplus and E. Shakhnovich, Protein folding: Theoretical studies, in Protein Folding, edited by T. Creighton, (Freeman, New York, 1992), pp. 127–195.en_US
dc.identifier.citedreferenceK. A. Dill et al., Protein Sci. 4, 561 (1995).en_US
dc.identifier.citedreferenceM. Karplus and A. Šali, Current Biology 5, 58 (1995).en_US
dc.identifier.citedreferenceP. G. Wolynes, Z. Luthey-Schulten, and J. N. Onuchic, Current Biology 3, 425 (1996).en_US
dc.identifier.citedreferenceJ. D. Bryngelson and P. G. Wolynes, Proc. Nat. Acad. Sci. U.S.A. 84, 7524 (1987).en_US
dc.identifier.citedreferenceJ. D. Bryngelson and P. G. Wolynes, J. Phys. Chem. 93, 6902 (1989).en_US
dc.identifier.citedreferenceJ. D. Bryngelson and P. G. Wolynes, Biopolymers 30, 171 (1990).en_US
dc.identifier.citedreferenceR. A. Goldstein, Z. A. Luthey-Schulten, and P. G. Wolynes, Proc. Nat. Acad. Sci., U.S.A. 89, 4918 (1992).en_US
dc.identifier.citedreferenceR. A. Goldstein, Z. A. Luthey-Schulten, and P. G. Wolynes, Proc. Nat. Acad. Sci., U.S.A. 89, 9029 (1992).en_US
dc.identifier.citedreferenceA. Šali, E. I. Shakhnovich, and M. J. Karplus, J. Mol. Biol. 235, 1614 (1994).en_US
dc.identifier.citedreferenceE. I. Shakhnovich, Phys. Rev. Lett. 72, 3907 (1994).en_US
dc.identifier.citedreferenceV. I. Abkevich, A. M. Gutin, and E. I. Shakhnovich, Biochem. 33, 10026 (1994).en_US
dc.identifier.citedreferenceD. Thirumalai, J. Phys. I France. 5, 1457 (1995).en_US
dc.identifier.citedreferenceD. K. Klimov and D. Thirumalai, Phys. Rev. Lett. 76, 4070 (1996).en_US
dc.identifier.citedreferenceS. Govindarajan and R. A. Goldstein, Biopolymers 36, 43 (1995).en_US
dc.identifier.citedreferenceJ. N. Onuchic, P. G. Wolynes, Z. Luthey-Schulten, and N. D. Socci, Proc. Nat. Acad. Sci., U.S.A. 92, 3626 (1995).en_US
dc.identifier.citedreferenceN. D. Socci, J. N. Onuchic, and P. G. Wolynes, J. Chem. Phys. 104, 5860 (1996).en_US
dc.identifier.citedreferenceS. Govindarajan and R. A. Goldstein, Proteins 22, 413 (1995).en_US
dc.identifier.citedreferenceJ. M. Koshi and R. A. Goldstein, Proteins 27, 336 (1997).en_US
dc.identifier.citedreferenceP. J. Flory, J. Chem. Phys. 17, 303 (1949).en_US
dc.identifier.citedreferenceI. C. Sanchez, Macromolecules 12, 980 (1979).en_US
dc.identifier.citedreferenceV. I. Abkevich, A. M. Gutin, and E. I. Shakhnovich, Folding and Design 1, 221 (1996).en_US
dc.identifier.citedreferenceJ. D. Bryngelson, J. N. Onuchic, N. D. Socci, and P. G. Wolynes, Proteins 21, 167 (1995).en_US
dc.identifier.citedreferenceK. J. Laidler, Chemical Kinetics, 3rd ed. (Harper & Row, New York, 1987).en_US
dc.identifier.citedreferenceA. F. Chaffotte, Y. Guillou, M. Delepierre, H.-J. Hinz, and M. E. Goldberg, Biochem. 30, 8067 (1991).en_US
dc.identifier.citedreferenceA. F. Chaffotte, C. Cadieux, Y. Guillou, and M. E. Goldberg, Biochem. 31, 4303 (1992).en_US
dc.identifier.citedreferenceL. S. Itzhaki, P. A. Evans, C. M. Dobson, and S. E. Radford, Biochem. 33, 5212 (1994).en_US
dc.identifier.citedreferenceV. R. Agashe, M. C. R. Shastry, and J. B. Udgaonkar, Nature 377, 754 (1995).en_US
dc.identifier.citedreferenceW. A. Houry, D. M. Rothwarf, and H. A. Scheraga, Biochem. 35, 10125 (1996).en_US
dc.identifier.citedreferenceE. I. Shakhnovich, G. Farztdinov, A. M. Gutin, and M. Karplus, Phys. Rev. Lett. 67, 1665 (1991).en_US
dc.identifier.citedreferenceC. J. Camacho and D. Thirumalai, Phys. Rev. Lett. 71, 2505 (1993).en_US
dc.identifier.citedreferenceC. J. Camacho and D. Thirumalai, Proc. Nat. Acad. Sci., U. S. A. 90, 6369 (1993).en_US
dc.identifier.citedreferenceM. Fukugita, D. Lancaster, and M. G. Mitchard, Proc. Nat. Acad. Sci., U. S. A. 90, 6365 (1993).en_US
dc.identifier.citedreferenceN. D. Socci and J. N. Onuchic, J. Chem. Phys. 101, 1519 (1994).en_US
dc.identifier.citedreferenceA. M. Gutin, V. I. Abkevich, and E. I. Shakhnovich, Biochem. 34, 3066 (1995).en_US
dc.identifier.citedreferenceS. Kamtekar, J. M. Schiffer, H. Xiong, J. M. Babik, and M. H. Hecht, Science 262, 1680 (1993).en_US
dc.identifier.citedreferenceM. W. West and M. H. Hecht, Protein Sci. 4, 2032 (1995).en_US
dc.owningcollnamePhysics, Department of


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