TY - JOUR
T1 - ITC in the post-genomic era...? Priceless
AU - Velazquez-Campoy, Adrián
AU - Freire, Ernesto
N1 - Funding Information:
This work was supported by grants GM 57144 and GM 56550 from the National Institutes of Health and grant MCB-0131241 from the National Science Foundation. A.V.C. is a recipient of a Ramón y Cajal Research Contract from the Spanish Ministry of Science and Technology.
PY - 2005/4/1
Y1 - 2005/4/1
N2 - The information available after decoding the genome of the human species and many others is opening the possibility of new approaches to target thousands of protein interactions critical for a continuously increasing list of genetic and infectious diseases and pathologies, and to understand complex regulatory pathways and interaction networks describing cell function and interrelation. There is a need for a reliable technique offering the capability of measuring accurately macromolecular interactions (e.g. protein/ligand, protein/protein, protein/nucleic acid) in the laboratory. Compared to other analytical techniques, isothermal titration calorimetry (ITC) exhibits some important advantages for characterizing intermolecular interactions and binding equilibria. ITC is suitable for characterizing both low affinity interactions (e.g. protein network regulation and natural ligands) and high affinity interactions (e.g. rational drug design). Considering the advanced technological level reached as well as the outstanding quality of the information accessible through this technique, ITC is expected to play a very prominent role in the next years in the areas of rational drug design and protein network regulation.
AB - The information available after decoding the genome of the human species and many others is opening the possibility of new approaches to target thousands of protein interactions critical for a continuously increasing list of genetic and infectious diseases and pathologies, and to understand complex regulatory pathways and interaction networks describing cell function and interrelation. There is a need for a reliable technique offering the capability of measuring accurately macromolecular interactions (e.g. protein/ligand, protein/protein, protein/nucleic acid) in the laboratory. Compared to other analytical techniques, isothermal titration calorimetry (ITC) exhibits some important advantages for characterizing intermolecular interactions and binding equilibria. ITC is suitable for characterizing both low affinity interactions (e.g. protein network regulation and natural ligands) and high affinity interactions (e.g. rational drug design). Considering the advanced technological level reached as well as the outstanding quality of the information accessible through this technique, ITC is expected to play a very prominent role in the next years in the areas of rational drug design and protein network regulation.
KW - Binding equilibrium
KW - Extreme binding affinity
KW - Isothermal titration calorimetry
KW - Thermodynamics
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U2 - 10.1016/j.bpc.2004.12.015
DO - 10.1016/j.bpc.2004.12.015
M3 - Article
C2 - 15752592
AN - SCOPUS:14744271960
SN - 0301-4622
VL - 115
SP - 115
EP - 124
JO - Biophysical Chemistry
JF - Biophysical Chemistry
IS - 2-3 SPEC. ISS.
ER -