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Origin of the anomalous circular dichroism spectra of many apomyoglobin mutants
(Academic Press Inc Elsevier ScienceSan DiegoEUA, 2004)
Identification of folding intermediates of streblin, the most stable serine protease: biophysical analysis
(Humana Press Inc, 2014-01-01)
Streblin, a serine proteinase from plant Streblus asper, has been used to investigate the conformational changes induced by pH, temperature, and chaotropes. The near/far UV circular dichroism activities under fluorescence ...
Fast purification of the Apo form and of a non-binding heme mutant of recombinant sperm whale myoglobin
(Academic Press Inc Elsevier ScienceSan DiegoEUA, 2003)
Stability and folding studies of the N-domain of troponin C. Evidence for the formation of an intermediate
(Elsevier Science IncNew YorkEUA, 2004)
UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates
(National Academy of Sciences, 2002-12)
Protein folding in the cell involves the action of different molecular chaperones and folding-facilitating enzymes. In the endoplasmic reticulum (ER), the folding status of glycoproteins is stringently controlled by a ...
On the difference in stability between horse and sperm whale myoglobins
(Elsevier Science IncNew YorkEUA, 2005)
Three-Dimensional Domain Swapping Changes the Folding Mechanism of the Forkhead Domain of FoxP1
(Cell Press, 2016)
The forkhead family of transcription factors (Fox) controls gene transcription during key processes such as regulation of metabolism, embryogenesis, and immunity. Structurally, Fox proteins feature a conserved DNA-binding ...