Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM023303-21
Application #
2174070
Study Section
Special Emphasis Panel (ZRG3-PB (01))
Project Start
1976-05-01
Project End
1999-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
21
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Pennsylvania State University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
University Park
State
PA
Country
United States
Zip Code
16802
Watson, Matthew D; Peran, Ivan; Zou, Junjie et al. (2017) Selenomethionine Quenching of Tryptophan Fluorescence Provides a Simple Probe of Protein Structure. Biochemistry 56:1085-1094
Kathuria, Sagar V; Chan, Yvonne H; Nobrega, R Paul et al. (2016) Clusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability. Protein Sci 25:662-75
Peran, Ivan; Watson, Matthew D; Bilsel, Osman et al. (2016) Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure. Chem Commun (Camb) 52:2055-8
Rosen, Laura E; Kathuria, Sagar V; Matthews, C Robert et al. (2015) Non-native structure appears in microseconds during the folding of E. coli RNase H. J Mol Biol 427:443-53
Zhou, Huan-Xiang; Bilsel, Osman (2014) SAXS/SANS probe of intermolecular interactions in concentrated protein solutions. Biophys J 106:771-3
Kathuria, Sagar V; Kayatekin, Can; Barrea, Raul et al. (2014) Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS. J Mol Biol 426:1980-94
Graceffa, Rita; Nobrega, R Paul; Barrea, Raul A et al. (2013) Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam. J Synchrotron Radiat 20:820-5
Kathuria, Sagar V; Chan, Alexander; Graceffa, Rita et al. (2013) Advances in turbulent mixing techniques to study microsecond protein folding reactions. Biopolymers 99:888-96
Gangadhara, Basavanapura N; Laine, Jennifer M; Kathuria, Sagar V et al. (2013) Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein. J Mol Biol 425:1065-81
Das, Payel; Kapoor, Divya; Halloran, Kevin T et al. (2013) Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study. J Am Chem Soc 135:1882-90

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