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. Author manuscript; available in PMC: 2010 May 1.
Published in final edited form as: Biotechnol Bioeng. 2009 May 1;103(1):77–84. doi: 10.1002/bit.22221

Table 1.

Kinetic and thermodynamic parameters derived from amide H/D exchange experiments for subtilisin and for various subtilisin-lactose conjugates.

Subtilisin-Lactosea A1b kHX,1 (min−1) A2b kHX,2 (min−1) ΔGHX,1c (kcal/mol) (ΔGHX,1)−1 d (mol/kcal)
0.0 ± 0.0 0.52 1.39 0.48 0.0008 2.43 0.411
1.0 ± 0.1 0.40 1.40 0.60 0.0005 2.43 0.412
2.2 ± 0.1 0.28 1.19 0.72 0.0004 2.52 0.397
3.5 ± 0.6 0.16 0.27 0.83 0.0002 3.32 0.301
a

Average moles of lactose bound per mol of subtilisin.

b

Ai is the fraction of amide protons that exchange with the rate constant kHX,i.

c

Gibbs free-energy of unfolding per mol of peptide hydrogen.

d

Protein mobility.