Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
7R01GM045859-06
Application #
2022462
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1991-09-01
Project End
1998-08-31
Budget Start
1996-09-01
Budget End
1997-08-31
Support Year
6
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Texas Agrilife Research
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
110521739
City
College Station
State
TX
Country
United States
Zip Code
77843
Young, A C; Zhang, W; Sacchettini, J C et al. (1995) MHC class I-peptide interactions and TCR recognition. Cancer Surv 22:17-36
Young, A C; Nathenson, S G; Sacchettini, J C (1995) Structural studies of class I major histocompatibility complex proteins: insights into antigen presentation. FASEB J 9:26-36
Tarshis, L C; Yan, M; Poulter, C D et al. (1994) Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution. Biochemistry 33:10871-7
Young, A C; Zhang, W; Sacchettini, J C et al. (1994) The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection. Cell 76:39-50
Schreiber-Agus, N; Chin, L; Chen, K et al. (1994) Evolutionary relationships and functional conservation among vertebrate Max-associated proteins: the zebra fish homolog of Mxi1. Oncogene 9:3167-77
Mikami, B; Degano, M; Hehre, E J et al. (1994) Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis. Biochemistry 33:7779-87
Young, A C; Scapin, G; Kromminga, A et al. (1994) Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids. Structure 2:523-34
Dewan, J C; Grant, G A; Sacchettini, J C (1994) Crystal structure of kappa-bungarotoxin at 2.3-A resolution. Biochemistry 33:13147-54
Scapin, G; Young, A C; Kromminga, A et al. (1993) High resolution X-ray studies of mammalian intestinal and muscle fatty acid-binding proteins provide an opportunity for defining the chemical nature of fatty acid: protein interactions. Mol Cell Biochem 123:3-13
Eads, J; Sacchettini, J C; Kromminga, A et al. (1993) Escherichia coli-derived rat intestinal fatty acid binding protein with bound myristate at 1.5 A resolution and I-FABPArg106-->Gln with bound oleate at 1.74 A resolution. J Biol Chem 268:26375-85

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