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Proceedings 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 KoshlandScience (New York, N.Y.)|July 7, 1989
Influence of interior packing and hydrophobicity on the stability of a proteinW S Sandberg, T C TerwilligerProceedings of the National Academy of Sciences of the United States of America|August 1, 1993
Genetic fusion of subunits of a dimeric protein substantially enhances its stability and rate of foldingH Liang, W S Sandberg, 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 TerwilligerThe Journal of Biological Chemistry|August 15, 1986
Kinetics of receptor modification. The multiply methylated aspartate receptors involved in bacterial chemotaxisT C Terwilliger, J Y Wang, D E KoshlandProceedings of the National Academy of Sciences of the United States of America|September 1, 1986
Surface structure recognized for covalent modification of the aspartate receptor in chemotaxisT C Terwilliger, J Y Wang, D E KoshlandPageof 39