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Protein dynamics in cells may be different from those in dilute solutions in vitro, because the environment in cells is highly… Expand To understand how proteins fold in vivo, it is important to investigate the effects of macromolecular crowding on protein folding… Expand To investigate the consequences of macromolecular crowding on the behavior of a globular protein, we performed a combined… Expand Many native proteins occasionally form partially unfolded forms (PUFs), which can be detected by hydrogen/deuterium exchange and… Expand The folding kinetics of the 179-residue Azotobacter vinelandii apoflavodoxin, which has an alpha-beta parallel topology, have… Expand Many flavoproteins are non-covalent complexes between FMN and an apoprotein. To understand better the stability of flavoproteins… Expand The denaturant‐induced (un)folding of apoflavodoxin from Azotobacter vinelandii has been followed at the residue level by NMR… Expand A flavodoxin from Azotobacter vinelandii is chosen as a model system to study the folding of α/ß doubly wound proteins. The… Expand Flavodoxins are α/β proteins that mediate electron transfer reactions. The conformational stability of apoflavodoxin from Anabœna… Expand Abstract A method is described for determining riboflavin 5′-phosphate (FMN) and flavin adenine dinucleotide (FAD) in mixtures by… Expand