Subscribe to our Newsletter and get informed about new publication regulary and special discounts for subscribers!

ILCPA > Volume 3 > Theoretical Approach to the Common Events in Every...
< Back to Volume

Theoretical Approach to the Common Events in Every Living Cell - Protein Folding and Protein Misfolding

Full Text PDF


Folding and unfolding are crucial ways of regulating biological activity and targeting proteins to different cellular locations. Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a wide range of highly debilitating and increasingly prevalent diseases. Protein misfolding is a common event in living cells. Molecular chaperones not only assist protein folding; they also facilitate the degradation of misfolded polypeptides. Protein folding is governed solely by the protein itself, scientists discovered that some proteins have helped in the process called chaperones. When the intracellular degradative capacity is exceeded, juxtanuclear aggresomes are formed to sequester misfolded proteins. Misfolding of newly formed proteins not only results in a loss of physiological function of the protein but also may lead to the intra- or extra- cellular accumulation of that protein. A number of diseases have been shown to be characterised by the accumulation of misfolded proteins, notable example being Alzheimer's disease.


International Letters of Chemistry, Physics and Astronomy (Volume 3)
V.K. Vaibhav and S.L. Sachin, "Theoretical Approach to the Common Events in Every Living Cell - Protein Folding and Protein Misfolding", International Letters of Chemistry, Physics and Astronomy, Vol. 3, pp. 41-51, 2012
Online since:
Sep 2013

[1] Christopher M. Dobson, R. John Ellis, The EMBO Journal 17 (1998) 5251-5254.

[2] Radouil Tzekov, Linda Stein, Shalesh Kaushal. Cold Spring Harb Perspect Biol 3 a007492 (2011) 1-10.

[3] Feng Zhao, Jian Peng, Jinbo Xu, Bioinformatics 26(12) (2010) i310-i317.

[4] Hironobu Naiki, Yoshitaka Nagai, J Biochem 146(6) (2009) 751-756.

[5] Ashish Arora, Dennis Rinehart, Gabor Szabo, Lukas K., Tamm, The Journal of Biological Chemistry 275(3) (2000) 1594-1600.

[6] Lisa D. Cabrita, Christopher M. Dobson, John Christodoulou, Current Opinion in Structural Biology 20 (1) (2010) 33-45.

DOI: 10.1016/

[7] Yun-Tzai Lee, Tz-Hsiang Su, Wei-Cheng Lo1, Ping-Chiang Lyu, Shih-Che Sue, Circular Permutation Prediction Reveals a Viable Backbone Disconnection for Split Proteins: An Approach in Identifying a New Functional Split Intein PLOS One 8, e43820 (2012).

DOI: 10.1371/journal.pone.0043820

[8] Lila M. Gierasch, Protein Science 20 (2011) 783-790.

[9] William R Skach, Nature Structural & Molecular Biology 16(6) (2009) 606-612.

[10] Peter L. Freddolino, Christopher B. Harrison, Yanxin Liu, and Klaus Schulten, Nat Phys. 6(10) (2011) 751-758.

DOI: 10.1038/nphys1713

[11] Ferenc Orosz, Judit Ovádi, Bioinformatics 27(11) (2011) 1449-1454.

DOI: 10.1093/bioinformatics/btr175

[12] Yien Che Tsai, Allan M. Weissman, Genes & Cancer 17 (2010) 764-778.

[13] Jeung-Hoi Ha, Stewart N. Loh, Chemistry 25 18(26) (2012) 7984-7999.

DOI: 10.1002/chem.201200348

[14] John H. Van Drie, Chin J Cancer 30(2) (2011) 124-137.

Show More Hide