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Acta Crystallographica. Section D, Biological Crystallography|September 1, 1995
Difference refinement: obtaining differences between two related structuresT C Terwilliger, J BerendzenProceedings of the National Academy of Sciences of the United States of America|October 1, 1996
Potential use of additivity of mutational effects in simplifying protein engineeringM M Skinner, T C TerwilligerJournal of Molecular Biology|May 20, 1991
Isolation and in vitro characterization of temperature-sensitive mutants of the bacteriophage f1 gene V proteinH B Zabin, T C TerwilligerThe Journal of General Physiology|May 1, 1981
Osmotic water permeability of human red cellsT C Terwilliger, A K SolomonThe Journal of Biological Chemistry|June 25, 1984
Sites of methyl esterification and deamination on the aspartate receptor involved in chemotaxisT C Terwilliger, D E KoshlandBiophysical Journal|January 1, 1982
The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activitiesT C Terwilliger, L Weissman, D EisenbergProceedings of the National Academy of Sciences of the United States of America|January 1, 1984
The hydrophobic moment detects periodicity in protein hydrophobicityD Eisenberg, R M Weiss, T C TerwilligerNature|September 23, 1982
The helical hydrophobic moment: a measure of the amphiphilicity of a helixD Eisenberg, R M Weiss, T C TerwilligerNucleic Acids Research|September 26, 1988
A genetic selection for temperature-sensitive variants of the gene V protein of bacteriophage f1T C Terwilliger, W D Fulford, H B ZabinBiochemistry|June 25, 1991
Approaches to predicting effects of single amino acid substitutions on the function of a proteinH B Zabin, M P Horvath, T C TerwilligerPageof 7