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L N Lin

Showing results (1-10 of 33) with videos related to

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Biochemistry|June 24, 1980
Kinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific proteaseL N Lin, J F Brandts
Biochemistry|September 13, 1983
Evidence showing that a proline-specific endopeptidase has an absolute requirement for a trans peptide bond immediately preceding the active bondL N Lin, J F Brandts
Biochemistry|June 16, 1987
Evidence for the existence of three or more slow phases in the refolding of ribonuclease A and some characteristics of the phasesL N Lin, J F Brandts
Biochemistry|November 13, 1979
Role of cis-trans isomerism of the peptide bond in protease specificity. Kinetic studies on small proline-containing peptides and on polyprolineL N Lin, J F Brandts
Biochemistry|November 5, 1985
Isomer-specific proteolysis of model substrates: influence that the location of the proline residue exerts on cis/trans specificityL N Lin, J F Brandts
Methods in Enzymology|January 1, 1986
Proline isomerization studied with proteolytic enzymesJ F Brandts, L N Lin
Biochemistry|February 1, 1983
Determination of cis-trans proline isomerization by trypsin proteolysis. Application to a model pentapeptide and to oxidized ribonuclease AL N Lin, J F Brandts
Biochemistry|February 1, 1983
Mechanism for the unfolding and refolding of ribonuclease A. Kinetic studies utilizing spectroscopic methodsL N Lin, J F Brandts
Biochemistry|April 7, 1987
Refolding of ribonuclease in the presence and absence of ammonium sulfate pulses. Comparison between experiments and simulationsL N Lin, J F Brandts
Biochemistry|September 19, 1978
Further evidence suggesting that the slow phase in protein unfolding and refolding is due to proline isomerization: a kinetic study of carp parvalbuminsL N Lin, J F Brandts
Pageof 4

Showing results (1-10 of 33) with videos related to

Sort By:
Pageof 4
Biochemistry|June 24, 1980
Kinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific proteaseL N Lin, J F Brandts
Biochemistry|September 13, 1983
Evidence showing that a proline-specific endopeptidase has an absolute requirement for a trans peptide bond immediately preceding the active bondL N Lin, J F Brandts
Biochemistry|June 16, 1987
Evidence for the existence of three or more slow phases in the refolding of ribonuclease A and some characteristics of the phasesL N Lin, J F Brandts
Biochemistry|November 13, 1979
Role of cis-trans isomerism of the peptide bond in protease specificity. Kinetic studies on small proline-containing peptides and on polyprolineL N Lin, J F Brandts
Biochemistry|November 5, 1985
Isomer-specific proteolysis of model substrates: influence that the location of the proline residue exerts on cis/trans specificityL N Lin, J F Brandts
Methods in Enzymology|January 1, 1986
Proline isomerization studied with proteolytic enzymesJ F Brandts, L N Lin
Biochemistry|February 1, 1983
Determination of cis-trans proline isomerization by trypsin proteolysis. Application to a model pentapeptide and to oxidized ribonuclease AL N Lin, J F Brandts
Biochemistry|February 1, 1983
Mechanism for the unfolding and refolding of ribonuclease A. Kinetic studies utilizing spectroscopic methodsL N Lin, J F Brandts
Biochemistry|April 7, 1987
Refolding of ribonuclease in the presence and absence of ammonium sulfate pulses. Comparison between experiments and simulationsL N Lin, J F Brandts
Biochemistry|September 19, 1978
Further evidence suggesting that the slow phase in protein unfolding and refolding is due to proline isomerization: a kinetic study of carp parvalbuminsL N Lin, J F Brandts
Pageof 4