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J F Brandts

Showing results (1-10 of 57) with videos related to

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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
Biochemistry|February 1, 1983
Isomerization of proline-93 during the unfolding and refolding of ribonuclease AL N Lin, J F Brandts
Biochemistry|December 13, 1988
Separation of the nativelike intermediate from unfolded forms during refolding of ribonuclease AL N Lin, J F Brandts
Biochemistry|November 20, 1984
Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysisL N Lin, J F Brandts
Biochemistry|January 9, 1979
Evidence suggesting that some proteolytic enzymes may cleave only the trans form of the peptide bondL N Lin, J F Brandts
Biochemistry|February 1, 1983
Mechanism for the unfolding and refolding of ribonuclease A. Simulations using a simple model with no structural intermediatesL N Lin, J F Brandts
Archives of Biochemistry and Biophysics|October 1, 1978
The interaction of adenine nucleotides with the red cell membrane: a calorimetric studyP S Low, J F Brandts
Nature: New Biology|April 14, 1971
Natural abundance fourier transform of 13C nuclear magnetic resonance spectra of lysozymeJ C Chien, J F Brandts
Biochemistry|July 24, 1990
Study of strong to ultratight protein interactions using differential scanning calorimetryJ F Brandts, L N Lin
Methods in Enzymology|January 1, 1972
High precision capillary viscometryJ E McKie, J F Brandts
Pageof 6

Showing results (1-10 of 57) with videos related to

Sort By:
Pageof 6
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
Biochemistry|February 1, 1983
Isomerization of proline-93 during the unfolding and refolding of ribonuclease AL N Lin, J F Brandts
Biochemistry|December 13, 1988
Separation of the nativelike intermediate from unfolded forms during refolding of ribonuclease AL N Lin, J F Brandts
Biochemistry|November 20, 1984
Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysisL N Lin, J F Brandts
Biochemistry|January 9, 1979
Evidence suggesting that some proteolytic enzymes may cleave only the trans form of the peptide bondL N Lin, J F Brandts
Biochemistry|February 1, 1983
Mechanism for the unfolding and refolding of ribonuclease A. Simulations using a simple model with no structural intermediatesL N Lin, J F Brandts
Archives of Biochemistry and Biophysics|October 1, 1978
The interaction of adenine nucleotides with the red cell membrane: a calorimetric studyP S Low, J F Brandts
Nature: New Biology|April 14, 1971
Natural abundance fourier transform of 13C nuclear magnetic resonance spectra of lysozymeJ C Chien, J F Brandts
Biochemistry|July 24, 1990
Study of strong to ultratight protein interactions using differential scanning calorimetryJ F Brandts, L N Lin
Methods in Enzymology|January 1, 1972
High precision capillary viscometryJ E McKie, J F Brandts
Pageof 6