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Biochimica Et Biophysica Acta|September 27, 2000
Structure and function of alpha-fetoprotein: a biophysical overviewJ R Gillespie, V N UverskyProteins|October 12, 2000
Why are "natively unfolded" proteins unstructured under physiologic conditions?V N Uversky, J R Gillespie, A L FinkCellular and Molecular Life Sciences : CMLS|October 3, 2003
Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go?V N UverskyBiochemistry|December 7, 1993
Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globuleV N UverskyBiochemistry. Biokhimiia|April 29, 1998
Equilibrium unfolding of partially folded staphylococcal nuclease A2- and A3-forms is accompanied by the formation of an intermediate stateV N UverskyProteins|July 17, 2001
Denatured collapsed states in protein folding: example of apomyoglobinO Tcherkasskaya, V N UverskyJournal of Molecular Biology|January 12, 1996
Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperatureV N Uversky, O B PtitsynFEBS Letters|March 14, 1994
The molten globule is a third thermodynamical state of protein moleculesO B Ptitsyn, V N UverskyBiochemistry. Biokhimiia|April 29, 1998
Effect of natural ligands on the structural properties and conformational stability of proteinsV N Uversky, N V NarizhnevaBiochemistry. Biokhimiia|April 29, 1998
Decrease of dielectric constant transforms the protein molecule into the molten globule stateN V Narizhneva, V N UverskyPageof 11