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Robert Lee Van Etten

Affiliations: 
Purdue University, West Lafayette, IN, United States 
Area:
Biochemistry, Analytical Chemistry
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"Robert Lee Van Etten"
Bio:

DOI: 10.1021/ja01092a046
DOI: 10.1021/ja00962a043
DOI: 10.1021/ja00962a044
VAN ETTEN, ROBERT LEE (b. 1937), Associate Professor. B.S., 1959, Univ. of Chicago; Ph.D., 1965, Univ. of California, Davis. N.I.H. Postdoctoral Fellow, 1965-6, Northwestern Univ. Biochemistry. Enzyme mechanisms and enzyme models, comparative biochemistry of acid phosphatases and aryl sulfatases, bioorganic chemistry, deuterium solvent and kinetic isotope effects, oxygen- 18 isotope effects in carbon- 13 NMR spectroscopy.

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Parents

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Albert Thomas Bottini grad student 1965 UC Davis
 (On the stereochemistry of quaternization of amines.)
Myron L. Bender post-doc 1965-1966 Northwestern

Children

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Ming-Ming Zhou grad student 1998 Purdue
Dayin Lin grad student 2000 Purdue
Christin L. Thomas grad student 2003 Purdue

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Publications

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Gustafson CL, Stauffacher CV, Hallenga K, et al. (2005) Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop. Protein Science : a Publication of the Protein Society. 14: 2515-25
Thomas CL, McKinnon E, Granger BL, et al. (2002) Kinetic and spectroscopic studies of Tritrichomonas foetus low-molecular weight phosphotyrosyl phosphatase. Hydrogen bond networks and electrostatic effects. Biochemistry. 41: 15601-9
Akerud T, Thulin E, Van Etten RL, et al. (2002) Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding. Journal of Molecular Biology. 322: 137-52
Wang S, Tabernero L, Zhang M, et al. (2000) Crystal structures of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate Biochemistry. 39: 1903-1914
Wang S, Stauffacher CV, Van Etten RL. (2000) Structural and mechanistic basis for the activation of a low-molecular weight protein tyro sine phosphatase by adenine Biochemistry. 39: 1234-1242
Billet V, Van Etten RL, Bashford D. (2000) Stabilization of charges and protonation states in the active site of the protein tyrosine phosphatases: A computational study Journal of Physical Chemistry B. 104: 11321-11333
Tabernero L, Evans BN, Tishmack PA, et al. (1999) The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism. Biochemistry. 38: 11651-8
Zhou M, Van Etten RL. (1999) Structural basis of the tight binding of pyridoxal 5'-phosphate to a low molecular weight protein tyrosine phosphatase Biochemistry. 38: 2636-2646
Zhang M, Stauffacher CV, Lin D, et al. (1998) Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity. The Journal of Biological Chemistry. 273: 21714-20
Zhang Z, Ostanin K, Van Etten RL. (1997) Covalent modification and site-directed mutagenesis of an active site tryptophan of human prostatic acid phosphatase Acta Biochimica Polonica. 44: 659-672
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