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How strong are side chain interactions in the folding intermediate?
Samatova EN, Katina NS, Balobanov VA, Melnik BS, Dolgikh DA, Bychkova VE, Finkelstein AV. Samatova EN, et al. Among authors: melnik bs. Protein Sci. 2009 Oct;18(10):2152-9. doi: 10.1002/pro.229. Protein Sci. 2009. PMID: 19693934 Free PMC article.
The major mRNP protein YB-1: structural and association properties in solution.
Guryanov SG, Filimonov VV, Timchenko AA, Melnik BS, Kihara H, Kutyshenko VP, Ovchinnikov LP, Semisotnov GV. Guryanov SG, et al. Among authors: melnik bs. Biochim Biophys Acta. 2013 Feb;1834(2):559-67. doi: 10.1016/j.bbapap.2012.11.007. Epub 2012 Dec 5. Biochim Biophys Acta. 2013. PMID: 23220387
Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate state.
Melnik TN, Majorina MA, Larina DS, Kashparov IA, Samatova EN, Glukhov AS, Melnik BS. Melnik TN, et al. Among authors: melnik bs. PLoS One. 2014 Jun 3;9(6):e98645. doi: 10.1371/journal.pone.0098645. eCollection 2014. PLoS One. 2014. PMID: 24892675 Free PMC article.
60 results