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G Barany

Showing results (11-20 of 71) with videos related to

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Analytical Biochemistry|May 1, 1979
A chromatographic method for the quantitative analysis of the deprotection of dithiasuccinoyl (Dts) amino acidsG Barany, R B Merrifield
Methods in Enzymology|January 1, 1997
Handles for solid-phase peptide synthesisM F Songster, G Barany
Journal of the American Chemical Society|October 26, 1977
A new amino protecting group removable by reduction. Chemistry of the dithiasuccinoyl (Dts) functionG Barany, R B Merrifield
Methods in Enzymology|January 1, 1997
Disulfide bond formation in peptidesI Annis, B Hargittai, G Barany
Protein Science : a Publication of the Protein Society|September 23, 1997
Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitorH Pan, G Barany, C Woodward
International Journal of Peptide and Protein Research|September 1, 1992
Solid-phase synthesis of bovine pancreatic trypsin inhibitor (BPTI) and two analogues. A chemical approach for evaluating the role of disulfide bridges in protein folding and stabilityM Ferrer, C Woodward, G Barany
Biochemistry|July 13, 2000
Synthesis and characterization of a beta-hairpin peptide that represents a 'core module' of bovine pancreatic trypsin inhibitor (BPTI)N Carulla, C Woodward, G Barany
Biochemistry|September 12, 1995
Dynamic structure of a highly ordered beta-sheet molten globule: multiple conformations with a stable coreE Barbar, G Barany, C Woodward
Bioconjugate Chemistry|September 20, 2001
Toward new designed proteins derived from bovine pancreatic trypsin inhibitor (BPTI): covalent cross-linking of two 'core modules' by oxime-forming ligationN Carulla, C Woodward, G Barany
Nature Structural Biology|March 1, 1995
Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitorM Ferrer, G Barany, C Woodward
Pageof 8

Showing results (11-20 of 71) with videos related to

Sort By:
Pageof 8
Analytical Biochemistry|May 1, 1979
A chromatographic method for the quantitative analysis of the deprotection of dithiasuccinoyl (Dts) amino acidsG Barany, R B Merrifield
Methods in Enzymology|January 1, 1997
Handles for solid-phase peptide synthesisM F Songster, G Barany
Journal of the American Chemical Society|October 26, 1977
A new amino protecting group removable by reduction. Chemistry of the dithiasuccinoyl (Dts) functionG Barany, R B Merrifield
Methods in Enzymology|January 1, 1997
Disulfide bond formation in peptidesI Annis, B Hargittai, G Barany
Protein Science : a Publication of the Protein Society|September 23, 1997
Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitorH Pan, G Barany, C Woodward
International Journal of Peptide and Protein Research|September 1, 1992
Solid-phase synthesis of bovine pancreatic trypsin inhibitor (BPTI) and two analogues. A chemical approach for evaluating the role of disulfide bridges in protein folding and stabilityM Ferrer, C Woodward, G Barany
Biochemistry|July 13, 2000
Synthesis and characterization of a beta-hairpin peptide that represents a 'core module' of bovine pancreatic trypsin inhibitor (BPTI)N Carulla, C Woodward, G Barany
Biochemistry|September 12, 1995
Dynamic structure of a highly ordered beta-sheet molten globule: multiple conformations with a stable coreE Barbar, G Barany, C Woodward
Bioconjugate Chemistry|September 20, 2001
Toward new designed proteins derived from bovine pancreatic trypsin inhibitor (BPTI): covalent cross-linking of two 'core modules' by oxime-forming ligationN Carulla, C Woodward, G Barany
Nature Structural Biology|March 1, 1995
Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitorM Ferrer, G Barany, C Woodward
Pageof 8