Influence of Temperature on the Urea Denaturation of β-Lactoglobulin

Bovine β-lactoglobulins in urea solution. Denaturation at pH 5.2 and 3.5

“…The conclusions that the urea denaturation of 3-lactoglobulin is not a two-state process and that there may also be irreversible changes are in agreement with early studies on pooled 3'lactoglobulin (Jacobsen and Christensen, 1948;Linderstrpm-Lang, 1949, 1952Christensen, 1952;Johansen, 1953;, but are at variance with the findings of Pace and Tanford (1968) who concluded that the urea denaturation of bovine 3-lactoglobulin A is two state at pH 2.5-3.5, and that irreversible reactions do not play a role. Similar views have recently been expressed by Alexander and Pace (1971) for urea denaturation of bovine 3-lactoglobulins A and B and caprid 3-lactoglobulin.…”

Studies on the heterogeneity of crystallized β-lactoglobulin

“…Urea. An attempt was made to bring about a differential denaturation as described by Jacobsen & Christensen (1948). A solution (10 ml.)…”

The Cold Denatured State Is Compact but Expands at Low Temperatures: Hydrodynamic Properties of the Cold Denatured State of the C-terminal Domain of L9

“…There have been multiple attempts to reach the cold-denatured state without strongly perturbing the environment. Studies have been reported which monitor cold denaturation in the presence of denaturant 23,24 and of super-cooled Abbreviations used: CTL9, the C-terminal domain of the ribosomal protein L9; CTL9-I98A, isoleucine to alanine point mutant of CTL9 at residue 98; k f , the rate constant for protein folding; k obs , the observed first-order rate constant measured in a stopped-flow experiment; k u , the rate constant for protein unfolding; PFG-NMR, pulsed-field gradient nuclear magnetic resonance; R h , the radius of hydration; T m , the midpoint of the high temperature thermal unfolding transition.…”