Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM035393-12
Application #
2177880
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1985-07-01
Project End
1997-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
12
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
University of California Berkeley
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704

  Publications

Muratore, Kathryn E; Engelhardt, Barbara E; Srouji, John R et al. (2013) Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: recurrence of tyrosine aminotransferase activity in the I? subfamily. Proteins 81:1593-609
Shultzaberger, Ryan K; Maerkl, Sebastian J; Kirsch, Jack F et al. (2012) Probing the informational and regulatory plasticity of a transcription factor DNA-binding domain. PLoS Genet 8:e1002614
Deu, Edgar; Kirsch, Jack F (2011) Engineering homooligomeric proteins to detect weak intersite allosteric communication: aminotransferases, a case study. Protein Sci 20:1991-2003
Hanes, Melinda S; Reynolds, Kimberly A; McNamara, Case et al. (2011) Specificity and cooperativity at ?-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions. Proteins 79:1267-76
Sankararaman, Sriram; Sha, Fei; Kirsch, Jack F et al. (2010) Active site prediction using evolutionary and structural information. Bioinformatics 26:617-24
Deu, Edgar; Dhoot, Jashdeep; Kirsch, Jack F (2009) The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a ""molten interface"" structure. Biochemistry 48:433-41
Muratore, Kathryn E; Srouji, John R; Chow, Margaret A et al. (2008) Recombinant expression of twelve evolutionarily diverse subfamily Ialpha aminotransferases. Protein Expr Purif 57:34-44
Yin, Yifeng; Kirsch, Jack F (2007) Identification of functional paralog shift mutations: conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase. Proc Natl Acad Sci U S A 104:17353-7
Deu, Edgar; Kirsch, Jack F (2007) Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme. Biochemistry 46:5819-29
Reynolds, Kimberly A; Thomson, Jodi M; Corbett, Kevin D et al. (2006) Structural and computational characterization of the SHV-1 beta-lactamase-beta-lactamase inhibitor protein interface. J Biol Chem 281:26745-53

Showing the most recent 10 out of 72 publications