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J F Brandts

Showing results (11-20 of 57) 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|May 26, 1970
Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximationW M Jackson, 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
Molecular Pharmacology|July 1, 1979
Interaction of phenothiazines and lower aliphatic alcohols with erythrocyte membranes: a scanning calorimetric studyK S Krishnan, 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
Pageof 6

Showing results (11-20 of 57) with videos related to

Sort By:
Pageof 6
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|May 26, 1970
Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximationW M Jackson, 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
Molecular Pharmacology|July 1, 1979
Interaction of phenothiazines and lower aliphatic alcohols with erythrocyte membranes: a scanning calorimetric studyK S Krishnan, 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
Pageof 6