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Carl Frieden

Showing results (21-30 of 59) with videos related to

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Biochemistry|October 22, 2003
Consequences of single-site mutations in the intestinal fatty acid binding proteinMasoumeh Rajabzadeh, Jeff Kao, Carl Frieden
Proceedings of the National Academy of Sciences of the United States of America|February 11, 2005
The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methodsKrishnananda Chattopadhyay, Elliot L Elson, Carl Frieden
Proceedings of the National Academy of Sciences of the United States of America|June 1, 2017
A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactionsCarl Frieden, Hanliu Wang, Chris M W Ho
Proteins|July 17, 2010
Dry molten globule intermediates and the mechanism of protein unfoldingRobert L Baldwin, Carl Frieden, George D Rose
Biophysical Journal|November 24, 2004
Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopyKrishnananda Chattopadhyay, Saveez Saffarian, Elliot L Elson, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 17, 2002
Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopyKrishnananda Chattopadhyay, Saveez Saffarian, Elliot L Elson, et al.
Biochemistry|August 19, 2011
Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4Brian Gau, Kanchan Garai, Carl Frieden, et al.
Biochemistry|May 13, 2017
Deamidation Slows Curli Amyloid-Protein AggregationHanliu Wang, Qin Shu, Carl Frieden, et al.
Protein Science : a Publication of the Protein Society|November 12, 2009
Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMRKanchan Garai, Sourajit M Mustafi, Berevan Baban, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 17, 2002
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapDJames G Bann, Jerome Pinkner, Scott J Hultgren, et al.
Pageof 6

Showing results (21-30 of 59) with videos related to

Sort By:
Pageof 6
Biochemistry|October 22, 2003
Consequences of single-site mutations in the intestinal fatty acid binding proteinMasoumeh Rajabzadeh, Jeff Kao, Carl Frieden
Proceedings of the National Academy of Sciences of the United States of America|February 11, 2005
The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methodsKrishnananda Chattopadhyay, Elliot L Elson, Carl Frieden
Proceedings of the National Academy of Sciences of the United States of America|June 1, 2017
A mechanism for lipid binding to apoE and the role of intrinsically disordered regions coupled to domain-domain interactionsCarl Frieden, Hanliu Wang, Chris M W Ho
Proteins|July 17, 2010
Dry molten globule intermediates and the mechanism of protein unfoldingRobert L Baldwin, Carl Frieden, George D Rose
Biophysical Journal|November 24, 2004
Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopyKrishnananda Chattopadhyay, Saveez Saffarian, Elliot L Elson, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 17, 2002
Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopyKrishnananda Chattopadhyay, Saveez Saffarian, Elliot L Elson, et al.
Biochemistry|August 19, 2011
Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4Brian Gau, Kanchan Garai, Carl Frieden, et al.
Biochemistry|May 13, 2017
Deamidation Slows Curli Amyloid-Protein AggregationHanliu Wang, Qin Shu, Carl Frieden, et al.
Protein Science : a Publication of the Protein Society|November 12, 2009
Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMRKanchan Garai, Sourajit M Mustafi, Berevan Baban, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 17, 2002
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapDJames G Bann, Jerome Pinkner, Scott J Hultgren, et al.
Pageof 6