Title : Protein stability and structure in HIC: hydrogen exchange experiments and COREX calculations.

Pub. Date : 2011 Jan 4

PMID : 21117672






4 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Hydrogen exchange mass spectrometry (HXMS) coupled to proteolytic digestion has been used to probe the conformation of bovine beta-lactoglobulin (BLG), bovine alpha-lactalbumin (BLA), and human serum albumin (HSA) in solution and while adsorbed to the hydrophobic interaction chromatography media Phenyl Sepharose 6FF. Hydrogen beta-lactoglobulin Bos taurus
2 Hydrogen exchange mass spectrometry (HXMS) coupled to proteolytic digestion has been used to probe the conformation of bovine beta-lactoglobulin (BLG), bovine alpha-lactalbumin (BLA), and human serum albumin (HSA) in solution and while adsorbed to the hydrophobic interaction chromatography media Phenyl Sepharose 6FF. Hydrogen beta-lactoglobulin Bos taurus
3 The hydrogen-deuterium exchange patterns of BLG and BLA on the surface suggest a structure that resembles each protein"s respective solution phase molten globule state. Hydrogen beta-lactoglobulin Bos taurus
4 COREX, an algorithm used to compute protein folding stabilities, correctly predicts solution hydrogen-deuterium exchange patterns for BLG and offers insight into its adsorbed phase stabilities but is unreliable for BLA predictions. Hydrogen beta-lactoglobulin Bos taurus