Abstract

The plan is to measure the binding of CO2 to carbonic anhydrase on phototriggering, either from a specifically-bound site close to the active site of the protein or from solution. The students at Swarthmore have just started with the synthesis, which they hope to complete by the end of the month. One of the molecules should release CO2 and an inhibitor of the enzyme, and the other shold release just an inhibitor. We have not arrived at an analogous design for something that will release only CO2, but we are working on that problem as well. The experiment will measure the CO2 released and track its binding into the carbonic anhydrase reactive sites. The measurement will employ ultrafast infrared spectroscopy with which it has been demonstrated that CO2 can be easily measured through its asymmetric stretching mode near 2000cm-1.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001348-20
Application #
6480821
Study Section
Project Start
2001-08-01
Project End
2002-07-31
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
20
Fiscal Year
2001
Total Cost
$155,764
Indirect Cost

  Institution

Name
University of Pennsylvania
Department
Type
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104

  Publications

Sheth, Rahul A; Arellano, Ronald S; Uppot, Raul N et al. (2015) Prospective trial with optical molecular imaging for percutaneous interventions in focal hepatic lesions. Radiology 274:917-26
Roussakis, Emmanuel; Spencer, Joel A; Lin, Charles P et al. (2014) Two-photon antenna-core oxygen probe with enhanced performance. Anal Chem 86:5937-45
Courter, Joel R; Abdo, Mohannad; Brown, Stephen P et al. (2014) The design and synthesis of alanine-rich ?-helical peptides constrained by an S,S-tetrazine photochemical trigger: a fragment union approach. J Org Chem 79:759-68
Singh, Prabhat K; Kuroda, Daniel G; Hochstrasser, Robin M (2013) An ion's perspective on the molecular motions of nanoconfined water: a two-dimensional infrared spectroscopy study. J Phys Chem B 117:9775-84
Chuntonov, Lev; Ma, Jianqiang (2013) Quantum process tomography quantifies coherence transfer dynamics in vibrational exciton. J Phys Chem B 117:13631-8
Culik, Robert M; Annavarapu, Srinivas; Nanda, Vikas et al. (2013) Using D-Amino Acids to Delineate the Mechanism of Protein Folding: Application to Trp-cage. Chem Phys 422:
Kuroda, Daniel G; Bauman, Joseph D; Challa, J Reddy et al. (2013) Snapshot of the equilibrium dynamics of a drug bound to HIV-1 reverse transcriptase. Nat Chem 5:174-81
Lam, A R; Moran, S D; Preketes, N K et al. (2013) Study of the ?D-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation. J Phys Chem B 117:15436-43
Kuroda, Daniel G; Singh, Prabhat K; Hochstrasser, Robin M (2013) Differential hydration of tricyanomethanide observed by time resolved vibrational spectroscopy. J Phys Chem B 117:4354-64
Goldberg, Jacob M; Speight, Lee C; Fegley, Mark W et al. (2012) Minimalist probes for studying protein dynamics: thioamide quenching of selectively excitable fluorescent amino acids. J Am Chem Soc 134:6088-91

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