Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM051559-02
Application #
2190174
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1994-09-02
Project End
1997-08-31
Budget Start
1995-09-01
Budget End
1996-08-31
Support Year
2
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Harvard University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
071723621
City
Cambridge
State
MA
Country
United States
Zip Code
02138
Shaw, Bryan F; Schneider, Gregory F; Whitesides, George M (2012) Effect of surfactant hydrophobicity on the pathway for unfolding of ubiquitin. J Am Chem Soc 134:18739-45
Shaw, Bryan F; Schneider, Gregory F; Arthanari, Haribabu et al. (2011) Complexes of native ubiquitin and dodecyl sulfate illustrate the nature of hydrophobic and electrostatic interactions in the binding of proteins and surfactants. J Am Chem Soc 133:17681-95
Lee, Andrew; Mirica, Katherine A; Whitesides, George M (2011) Influence of fluorocarbon and hydrocarbon acyl groups at the surface of bovine carbonic anhydrase II on the kinetics of denaturation by sodium dodecyl sulfate. J Phys Chem B 115:1199-210
Lee, Andrew; Tang, Sindy K Y; Mace, Charles R et al. (2011) Denaturation of proteins by SDS and tetraalkylammonium dodecyl sulfates. Langmuir 27:11560-74
Mecinovic, Jasmin; Snyder, Phillip W; Mirica, Katherine A et al. (2011) Fluoroalkyl and alkyl chains have similar hydrophobicities in binding to the ""hydrophobic wall"" of carbonic anhydrase. J Am Chem Soc 133:14017-26
Snyder, Phillip W; Mecinovic, Jasmin; Moustakas, Demetri T et al. (2011) Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase. Proc Natl Acad Sci U S A 108:17889-94
Lee, Andrew; Whitesides, George M (2010) Analysis of inorganic polyphosphates by capillary gel electrophoresis. Anal Chem 82:6838-46
Shaw, Bryan F; Arthanari, Haribabu; Narovlyansky, Max et al. (2010) Neutralizing positive charges at the surface of a protein lowers its rate of amide hydrogen exchange without altering its structure or increasing its thermostability. J Am Chem Soc 132:17411-25
Krishnamurthy, Vijay M; Kaufman, George K; Urbach, Adam R et al. (2008) Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding. Chem Rev 108:946-1051
Schneider, Gregory F; Shaw, Bryan F; Lee, Andrew et al. (2008) Pathway for unfolding of ubiquitin in sodium dodecyl sulfate, studied by capillary electrophoresis. J Am Chem Soc 130:17384-93

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