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J Wedemeyer

Showing results (11-20 of 69) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|March 29, 2001
A role for intermolecular disulfide bonds in prion diseases?E Welker, W J Wedemeyer, H A Scheraga
Biochemistry|August 26, 1998
Proline isomerization in bovine pancreatic ribonuclease A. 1. Unfolding conditionsD Juminaga, W J Wedemeyer, H A Scheraga
The Journal of Physical Chemistry. B|November 17, 2010
A general polymer model of unfolded proteins under folding conditionsYujie Chen, William J Wedemeyer, Lisa J Lapidus
Biochemistry|March 3, 1999
Conformational unfolding studies of three-disulfide mutants of bovine pancreatic ribonuclease A and the coupling of proline isomerization to disulfide redox reactionsM Iwaoka, W J Wedemeyer, H A Scheraga
Research in Microbiology|July 6, 2010
Homology-based modeling of the Erwinia amylovora type III secretion chaperone DspF used to identify amino acids required for virulence and interaction with the effector DspELindsay R Triplett, William J Wedemeyer, George W Sundin
Journal of Biomolecular NMR|March 9, 2002
Exact solutions for chemical bond orientations from residual dipolar couplingsWilliam J Wedemeyer, Carol A Rohl, Harold A Scherag
Analytical Biochemistry|May 15, 1997
Kinetics of competitive binding with application to thrombin complexesW J Wedemeyer, R W Ashton, H A Scheraga
Biochemistry|April 12, 2000
Disulfide bonds and protein foldingW J Wedemeyer, E Welker, M Narayan, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 28, 2001
Structural determinants of oxidative folding in proteinsE Welker, M Narayan, W J Wedemeyer, et al.
Biophysical Journal|September 6, 2011
Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapieKai-Chun Chen, Ming Xu, William J Wedemeyer, et al.
Pageof 7

Showing results (11-20 of 69) with videos related to

Sort By:
Pageof 7
Proceedings of the National Academy of Sciences of the United States of America|March 29, 2001
A role for intermolecular disulfide bonds in prion diseases?E Welker, W J Wedemeyer, H A Scheraga
Biochemistry|August 26, 1998
Proline isomerization in bovine pancreatic ribonuclease A. 1. Unfolding conditionsD Juminaga, W J Wedemeyer, H A Scheraga
The Journal of Physical Chemistry. B|November 17, 2010
A general polymer model of unfolded proteins under folding conditionsYujie Chen, William J Wedemeyer, Lisa J Lapidus
Biochemistry|March 3, 1999
Conformational unfolding studies of three-disulfide mutants of bovine pancreatic ribonuclease A and the coupling of proline isomerization to disulfide redox reactionsM Iwaoka, W J Wedemeyer, H A Scheraga
Research in Microbiology|July 6, 2010
Homology-based modeling of the Erwinia amylovora type III secretion chaperone DspF used to identify amino acids required for virulence and interaction with the effector DspELindsay R Triplett, William J Wedemeyer, George W Sundin
Journal of Biomolecular NMR|March 9, 2002
Exact solutions for chemical bond orientations from residual dipolar couplingsWilliam J Wedemeyer, Carol A Rohl, Harold A Scherag
Analytical Biochemistry|May 15, 1997
Kinetics of competitive binding with application to thrombin complexesW J Wedemeyer, R W Ashton, H A Scheraga
Biochemistry|April 12, 2000
Disulfide bonds and protein foldingW J Wedemeyer, E Welker, M Narayan, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 28, 2001
Structural determinants of oxidative folding in proteinsE Welker, M Narayan, W J Wedemeyer, et al.
Biophysical Journal|September 6, 2011
Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapieKai-Chun Chen, Ming Xu, William J Wedemeyer, et al.
Pageof 7