Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM034171-13
Application #
2177319
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1982-05-01
Project End
1999-04-30
Budget Start
1996-05-01
Budget End
1997-04-30
Support Year
13
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Johns Hopkins University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
045911138
City
Baltimore
State
MD
Country
United States
Zip Code
21218
Shortle, D (1994) Assignment of amino acid type in 1H-15N correlation spectra by labeling with 14N-amino acids. J Magn Reson B 105:88-90
Stites, W E; Meeker, A K; Shortle, D (1994) Evidence for strained interactions between side-chains and the polypeptide backbone. J Mol Biol 235:27-32
Alexandrescu, A T; Abeygunawardana, C; Shortle, D (1994) Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study. Biochemistry 33:1063-72
Alexandrescu, A T; Shortle, D (1994) Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease. J Mol Biol 242:527-46
Shortle, D; Abeygunawardana, C (1993) NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. Structure 1:121-34
Gittis, A G; Stites, W E; Lattman, E E (1993) The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order. J Mol Biol 232:718-24
Li, Y K; Kuliopulos, A; Mildvan, A S et al. (1993) Environments and mechanistic roles of the tyrosine residues of delta 5-3-ketosteroid isomerase. Biochemistry 32:1816-24
Green, S M; Shortle, D (1993) Patterns of nonadditivity between pairs of stability mutations in staphylococcal nuclease. Biochemistry 32:10131-9
Sondek, J; Shortle, D (1992) A general strategy for random insertion and substitution mutagenesis: substoichiometric coupling of trinucleotide phosphoramidites. Proc Natl Acad Sci U S A 89:3581-5
Green, S M; Meeker, A K; Shortle, D (1992) Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: evidence for mutational effects on the free energy of the denatured state. Biochemistry 31:5717-28

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