Subject(s)
Autophagy , Saccharomyces cerevisiae Proteins/metabolism , Saccharomyces cerevisiae/enzymology , TOR Serine-Threonine Kinases/history , History, 20th Century , History, 21st Century , Microscopy, Electron, Transmission , Mutation , Nobel Prize , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/ultrastructure , Saccharomyces cerevisiae Proteins/genetics , Saccharomyces cerevisiae Proteins/history , TOR Serine-Threonine Kinases/genetics , TOR Serine-Threonine Kinases/metabolism , Vacuoles/metabolism , Vacuoles/ultrastructureSubject(s)
Proliferating Cell Nuclear Antigen/metabolism , Saccharomyces cerevisiae Proteins/metabolism , Saccharomyces cerevisiae/metabolism , Ubiquitin-Conjugating Enzymes/metabolism , Ubiquitin/metabolism , Ubiquitination/physiology , Animals , History, 20th Century , History, 21st Century , Humans , Proliferating Cell Nuclear Antigen/genetics , Proliferating Cell Nuclear Antigen/history , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae Proteins/genetics , Saccharomyces cerevisiae Proteins/history , Ubiquitin/genetics , Ubiquitin/history , Ubiquitin-Conjugating Enzymes/genetics , Ubiquitin-Conjugating Enzymes/historySubject(s)
Actin Cytoskeleton/metabolism , Cell Cycle Proteins/history , Cell Polarity/genetics , Guanine Nucleotide Exchange Factors/history , Saccharomyces cerevisiae Proteins/history , Saccharomyces cerevisiae/metabolism , cdc42 GTP-Binding Protein, Saccharomyces cerevisiae/history , History, 20th Century , HumansSubject(s)
Munc18 Proteins/genetics , Saccharomyces cerevisiae Proteins/genetics , Saccharomyces cerevisiae/genetics , Animals , History, 20th Century , History, 21st Century , Humans , Molecular Biology/history , Munc18 Proteins/history , Munc18 Proteins/ultrastructure , Saccharomyces cerevisiae Proteins/history , Saccharomyces cerevisiae Proteins/ultrastructureABSTRACT
Peptide models have been widely used to investigate conformational aspects of domains of proteins since the early 1950s. A pioneer in this field was Dr. Murray Goodman, who applied a battery of methodologies to study the onset of structure in homooligopeptides. This article reviews some of Dr. Goodman's contributions, and reports recent studies using linear and constrained peptides corresponding to the first extracellular loop and linear peptides corresponding to the sixth transmembrane domain of a G-protein coupled receptor from the yeast Saccharomyces cerevisiae. Peptides containing 30-40 residues were synthesized using solid-phase methods and purified to near homogeneity by reversed phase high performance liquid chromatography. CD and NMR analyses indicated that the first extracellular loop peptides were mostly flexible in water, and assumed some helical structure near the N-terminus in trifluoroethanol and in the presence of micelles. Comparison of oligolysines with native loop residues revealed that three lysines at each terminus of a peptide corresponding to the sixth transmembrane domain of the alpha-factor receptor resulted in better aqueous solubility and greater helicity than the native loop residues.