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Biochemical Society Symposium|September 28, 2001
Defining the structure of the substrate-free state of the DnaK molecular chaperoneJ F Swain, R Sivendran, L M GieraschThe Journal of Biological Chemistry|October 15, 1989
Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical propertiesC J McKnight, M S Briggs, L M GieraschBiochemistry|October 17, 1989
Helix formation and stability in a signal sequenceM D Bruch, C J McKnight, L M GieraschBiopolymers|December 1, 1992
Solution conformations of two flexible cyclic pentapeptides: cyclo(Gly-Pro-D-Phe-Gly-Ala) and cyclo(Gly-Pro-D-Phe-Gly-Val)A N Stroup, A L Rockwell, L M GieraschProteins|January 1, 1991
Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase AM D Bruch, M M Dhingra, L M GieraschJournal of Molecular Biology|February 20, 1999
Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain couplingD L Montgomery, R I Morimoto, L M GieraschFolding & Design|November 10, 1998
Probing the folding pathway of a beta-clam protein with single-tryptophan constructsP L Clark, B F Weston, L M GieraschJournal of Bioenergetics and Biomembranes|June 1, 1990
Biophysical studies of signal peptides: implications for signal sequence functions and the involvement of lipid in protein exportJ D Jones, C J McKnight, L M GieraschPeptide Research|September 1, 1989
T-cell antigenic peptides from sperm whale myoglobin fold as amphipathic helices: a possible determinant for immunodominance?L R Lark, J A Berzofsky, L M GieraschPageof 10