Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 3571-3574 |
| Number of pages | 4 |
| Journal | Bulletin of the Chemical Society of Japan |
| Volume | 69 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 1996 |
| MoE publication type | A1 Journal article-refereed |
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Relation between the activity of catalytic antibodies and the properties of substrates. / Kodaka, Masato; Hase, Anneli.
In: Bulletin of the Chemical Society of Japan, Vol. 69, No. 12, 1996, p. 3571-3574.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Relation between the activity of catalytic antibodies and the properties of substrates
AU - Kodaka, Masato
AU - Hase, Anneli
PY - 1996
Y1 - 1996
N2 - The free energy of binding between catalytic antibodies and substrates is correlated with the properties of the substrates, both in the transition state (TS) and the ground state (GS). The free energy of binding was calculated from the kinetic parameters and four properties of the substrates; the solvent accessible surface area (SAS), enthalpy of hydration (ΔH), polarizability (α), and dipole moment (μ) were calculated using AM1. As a whole, TS shows a higher correlation than does GS, which is compatible with the fundamental concept of a catalytic antibody. Among these four properties, SAS gives the highest correlation coefficient (0.7616) while μ has a small correlation. Antibody-TS complexes seem to be stabilized by van der Waals force rather than a hydrophobic interaction.
AB - The free energy of binding between catalytic antibodies and substrates is correlated with the properties of the substrates, both in the transition state (TS) and the ground state (GS). The free energy of binding was calculated from the kinetic parameters and four properties of the substrates; the solvent accessible surface area (SAS), enthalpy of hydration (ΔH), polarizability (α), and dipole moment (μ) were calculated using AM1. As a whole, TS shows a higher correlation than does GS, which is compatible with the fundamental concept of a catalytic antibody. Among these four properties, SAS gives the highest correlation coefficient (0.7616) while μ has a small correlation. Antibody-TS complexes seem to be stabilized by van der Waals force rather than a hydrophobic interaction.
U2 - 10.1246/bcsj.69.3571
DO - 10.1246/bcsj.69.3571
M3 - Article
VL - 69
SP - 3571
EP - 3574
JO - Bulletin of the Chemical Society of Japan
JF - Bulletin of the Chemical Society of Japan
SN - 0009-2673
IS - 12
ER -