Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM039062-03
Application #
3295872
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1988-02-01
Project End
1990-06-30
Budget Start
1990-02-01
Budget End
1990-06-30
Support Year
3
Fiscal Year
1990
Total Cost
Indirect Cost
Name
Texas A&M University
Department
Type
Schools of Earth Sciences/Natur
DUNS #
City
College Station
State
TX
Country
United States
Zip Code
77845
Mascotti, D P; Lohman, T M (1997) Thermodynamics of oligoarginines binding to RNA and DNA. Biochemistry 36:7272-9
Mascotti, D P; Lohman, T M (1995) Thermodynamics of charged oligopeptide-heparin interactions. Biochemistry 34:2908-15
Mascotti, D P; Lohman, T M (1993) Thermodynamics of single-stranded RNA and DNA interactions with oligolysines containing tryptophan. Effects of base composition. Biochemistry 32:10568-79
Lohman, T M; Mascotti, D P (1992) Nonspecific ligand-DNA equilibrium binding parameters determined by fluorescence methods. Methods Enzymol 212:424-58
Lohman, T M; Mascotti, D P (1992) Thermodynamics of ligand-nucleic acid interactions. Methods Enzymol 212:400-24
Mascotti, D P; Lohman, T M (1992) Thermodynamics of single-stranded RNA binding to oligolysines containing tryptophan. Biochemistry 31:8932-46
Lohman, T M; Bujalowski, W (1991) Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor binding. Methods Enzymol 208:258-90
Mascotti, D P; Lohman, T M (1990) Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids. Proc Natl Acad Sci U S A 87:3142-6
Bujalowski, W; Lohman, T M; Anderson, C F (1989) On the cooperative binding of large ligands to a one-dimensional homogeneous lattice: the generalized three-state lattice model. Biopolymers 28:1637-43
Jezewska, M J; Bujalowski, W; Lohman, T M (1989) Iron(II)-ethylenediaminetetraacetic acid catalyzed cleavage of DNA is highly specific for duplex DNA. Biochemistry 28:6161-4

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