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Biochemistry|October 23, 1990
Reduced tendency to form a beta turn in peptides from the P22 tailspike protein correlates with a temperature-sensitive folding defectA N Stroup, L M GieraschBiochemistry|July 3, 1984
Exploring the conformational roles of signal sequences: synthesis and conformational analysis of lambda receptor protein wild-type and mutant signal peptidesM S Briggs, L M GieraschTrends in Biochemical Sciences|April 1, 1991
Recognition of nascent polypeptides for targeting and foldingS J Landry, L M GieraschThe Journal of Biological Chemistry|March 5, 1990
Comparison of helix stability in wild-type and mutant LamB signal sequencesM D Bruch, L M GieraschBiochemistry|July 30, 1991
The chaperonin GroEL binds a polypeptide in an alpha-helical conformationS J Landry, L M GieraschJournal of Molecular Biology|September 1, 2000
Multiple roles of prolyl residues in structure and foldingS J Eyles, L M GieraschBiophysical Journal|October 1, 1994
Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequenceJ D Jones, L M GieraschBiochemistry|June 25, 1991
Fluorescence analysis of tryptophan-containing variants of the LamB signal sequence upon insertion into a lipid bilayerC J McKnight, M Rafalski, L M GieraschThe Journal of Biological Chemistry|March 30, 2001
The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particleR M Cleverley, N Zheng, L M GieraschPageof 10