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M M Teeter

Showing results (31-40 of 38) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|March 29, 2000
Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambinC Jelsch, M M Teeter, V Lamzin, et al.
Protein Engineering|December 1, 1996
Expression, purification and characterization of recombinant crambinL Lobb, B Stec, E K Kantrowitz, et al.
Acta Crystallographica. Section D, Biological Crystallography|January 1, 1995
Crambin: a direct solution for a 400-atom structureC M Weeks, H A Hauptman, G D Smith, et al.
Journal of Molecular Biology|February 5, 1987
Nuclear magnetic resonance study of the solution structure of alpha 1-purothionin. Sequential resonance assignment, secondary structure and low resolution tertiary structureG M Clore, D K Sukumaran, A M Gronenborn, et al.
The Journal of Peptide Research : Official Journal of the American Peptide Society|December 23, 2004
Proposal for molecular mechanism of thionins deduced from physico-chemical studies of plant toxinsB Stec, O Markman, U Rao, et al.
Science (New York, N.Y.)|February 27, 1987
Solution of a protein crystal structure with a model obtained from NMR interproton distance restraintsA T Brünger, R L Campbell, G M Clore, et al.
Molecular Pharmacology|July 17, 2001
Modeling and mutational analysis of a putative sodium-binding pocket on the dopamine D2 receptorK A Neve, M G Cumbay, K R Thompson, et al.
Journal of Medicinal Chemistry|August 24, 2000
CoMFA-based prediction of agonist affinities at recombinant wild type versus serine to alanine point mutated D2 dopamine receptorsR E Wilcox, W H Huang, M Y Brusniak, et al.
Pageof 4

Showing results (31-40 of 38) with videos related to

Sort By:
Pageof 4
You have reached the last page of results.This site can display upto 38 results.
Proceedings of the National Academy of Sciences of the United States of America|March 29, 2000
Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambinC Jelsch, M M Teeter, V Lamzin, et al.
Protein Engineering|December 1, 1996
Expression, purification and characterization of recombinant crambinL Lobb, B Stec, E K Kantrowitz, et al.
Acta Crystallographica. Section D, Biological Crystallography|January 1, 1995
Crambin: a direct solution for a 400-atom structureC M Weeks, H A Hauptman, G D Smith, et al.
Journal of Molecular Biology|February 5, 1987
Nuclear magnetic resonance study of the solution structure of alpha 1-purothionin. Sequential resonance assignment, secondary structure and low resolution tertiary structureG M Clore, D K Sukumaran, A M Gronenborn, et al.
The Journal of Peptide Research : Official Journal of the American Peptide Society|December 23, 2004
Proposal for molecular mechanism of thionins deduced from physico-chemical studies of plant toxinsB Stec, O Markman, U Rao, et al.
Science (New York, N.Y.)|February 27, 1987
Solution of a protein crystal structure with a model obtained from NMR interproton distance restraintsA T Brünger, R L Campbell, G M Clore, et al.
Molecular Pharmacology|July 17, 2001
Modeling and mutational analysis of a putative sodium-binding pocket on the dopamine D2 receptorK A Neve, M G Cumbay, K R Thompson, et al.
Journal of Medicinal Chemistry|August 24, 2000
CoMFA-based prediction of agonist affinities at recombinant wild type versus serine to alanine point mutated D2 dopamine receptorsR E Wilcox, W H Huang, M Y Brusniak, et al.
Pageof 4