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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 ...
Structural modifications of beta-lactoglobulin subjected to gamma radiation
(Elsevier Sci LtdOxfordInglaterra, 2008)
Assessing native and non-native conformational states of a protein by methylene carbene labeling: the case of Bacillus licheniformis beta-lactamase
(American Chemical Society, 2007-11)
Much knowledge of protein folding can be derived from the examination of the nature and size of solvent-exposed surfaces along conformational transitions. We exploit here a general photochemical modification with methylene ...
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 ...
Experimentally Approaching the Solvent-Accessible Surface Area of a Protein: Insights into the Acid Molten Globule of Bovine α-Lactalbumin
(Academic Press Ltd - Elsevier Science Ltd, 2009-12)
Each conformational state of a protein is inextricably related to a defined extent of solvent exposure that plays a key role in protein folding and protein interactions. However, accurate measurement of the solvent-accessible ...
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 ...