Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM040384-09
Application #
2180298
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1988-07-01
Project End
2000-03-31
Budget Start
1996-04-01
Budget End
1997-03-31
Support Year
9
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Nebraska Lincoln
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
555456995
City
Lincoln
State
NE
Country
United States
Zip Code
68588
Wang, Lintao; Smith, David L (2005) Capsid structure and dynamics of a human rhinovirus probed by hydrogen exchange mass spectrometry. Protein Sci 14:1661-72
Wintrode, Patrick L; Rojsajjakul, Teerapat; Vadrevu, Ramakrishna et al. (2005) An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein. J Mol Biol 347:911-9
Raza, A S; Smith, D L (2004) Optimization of conditions for studies of protein unfolding by hydrogen exchange/mass spectrometry. Eur J Mass Spectrom (Chichester, Eng) 10:289-94
Swaim, Catherine L; Smith, Jean B; Smith, David L (2004) Unexpected products from the reaction of the synthetic cross-linker 3,3'-dithiobis(sulfosuccinimidyl propionate), DTSSP with peptides. J Am Soc Mass Spectrom 15:736-49
Pan, Hai; Smith, David L (2004) Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of Staphylococcus aureus aldolase. Methods Enzymol 380:285-308
Pan, Hai; Smith, David L (2003) Quaternary structure of aldolase leads to differences in its folding and unfolding intermediates. Biochemistry 42:5713-21
Wang, Lintao; Pan, Hai; Smith, David L (2002) Hydrogen exchange-mass spectrometry: optimization of digestion conditions. Mol Cell Proteomics 1:132-8
Wang, Lintao; Smith, David L (2002) Probing protein structure and dynamics by hydrogen exchange-mass spectrometry. Curr Protoc Protein Sci Chapter 17:Unit 17.6
Engen, J R; Smith, D L (2001) Investigating protein structure and dynamics by hydrogen exchange MS. Anal Chem 73:256A-265A
Chen, J; Smith, D L (2001) Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5. Protein Sci 10:1079-83

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