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Biochemistry|March 21, 1995
How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stabilityM Yao, D W BolenBiochemistry|October 18, 1988
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturantsM M Santoro, D W BolenBiochemistry|January 28, 1999
Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: implications regarding m values, intermediates, and thermodynamicsI V Baskakov, D W BolenJournal of Molecular Biology|August 15, 2001
The osmophobic effect: natural selection of a thermodynamic force in protein foldingD W Bolen, I V BaskakovBiochemistry|October 18, 1988
Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycleD W Bolen, M M SantoroProtein Science : a Publication of the Protein Society|July 1, 1999
The paradox between m values and deltaCp's for denaturation of ribonuclease T1 with disulfide bonds intact and brokenI V Baskakov, D W BolenBiophysical Chemistry|February 28, 1997
The Gibbs conference on biothermodynamics: origins and evolutionG K Ackers, D W BolenBiochemistry|May 26, 1992
A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration rangeM M Santoro, D W BolenBiophysical Chemistry|August 31, 1990
Calorimetric determination of linkage effects involving an acyl-enzyme intermediateD W Bolen, J L SlightomBiophysical Journal|May 20, 1998
Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesisI Baskakov, A Wang, D W BolenPageof 290