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S P Bottomley

Showing results (1-10 of 34) with videos related to

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Journal of Molecular Biology|November 9, 2001
Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded stateD J Tew, S P Bottomley
Biochemical and Biophysical Research Communications|January 13, 1998
The effects of reactive centre loop length upon serpin polymerisationS P Bottomley, W S Chang
Protein Engineering|February 4, 1999
Protein engineering of chimeric Serpins: an investigation into effects of the serpin scaffold and reactive centre loop lengthS P Bottomley, S R Stone
Current Medicinal Chemistry|July 16, 2010
Towards the treatment of polyglutamine diseases: the modulatory role of protein contextA L Robertson, S P Bottomley
FEBS Letters|April 12, 2001
Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibitionD J Tew, S P Bottomley
Archives of Biochemistry and Biophysics|August 15, 1998
The mechanism of alpha 1-antitrypsin polymerization probed by fluorescence spectroscopyE L James, S P Bottomley
Biochimica Et Biophysica Acta|August 30, 2000
The citrate ion increases the conformational stability of alpha(1)-antitrypsinS P Bottomley, D J Tew
The Journal of Biological Chemistry|July 6, 2000
Conformational change and intermediates in the unfolding of alpha 1-antichymotrypsinM C Pearce, H Rubin, S P Bottomley
Biological Chemistry|January 5, 2002
Osmolytes as modulators of conformational changes in serpinsM K Chow, G L Devlin, S P Bottomley
Biochemical and Biophysical Research Communications|October 29, 1998
Alpha 1-antitrypsin polymerisation can occur by both loop A and C sheet mechanismsS P Bottomley, P C Hopkins, J C Whisstock
Pageof 4

Showing results (1-10 of 34) with videos related to

Sort By:
Pageof 4
Journal of Molecular Biology|November 9, 2001
Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded stateD J Tew, S P Bottomley
Biochemical and Biophysical Research Communications|January 13, 1998
The effects of reactive centre loop length upon serpin polymerisationS P Bottomley, W S Chang
Protein Engineering|February 4, 1999
Protein engineering of chimeric Serpins: an investigation into effects of the serpin scaffold and reactive centre loop lengthS P Bottomley, S R Stone
Current Medicinal Chemistry|July 16, 2010
Towards the treatment of polyglutamine diseases: the modulatory role of protein contextA L Robertson, S P Bottomley
FEBS Letters|April 12, 2001
Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibitionD J Tew, S P Bottomley
Archives of Biochemistry and Biophysics|August 15, 1998
The mechanism of alpha 1-antitrypsin polymerization probed by fluorescence spectroscopyE L James, S P Bottomley
Biochimica Et Biophysica Acta|August 30, 2000
The citrate ion increases the conformational stability of alpha(1)-antitrypsinS P Bottomley, D J Tew
The Journal of Biological Chemistry|July 6, 2000
Conformational change and intermediates in the unfolding of alpha 1-antichymotrypsinM C Pearce, H Rubin, S P Bottomley
Biological Chemistry|January 5, 2002
Osmolytes as modulators of conformational changes in serpinsM K Chow, G L Devlin, S P Bottomley
Biochemical and Biophysical Research Communications|October 29, 1998
Alpha 1-antitrypsin polymerisation can occur by both loop A and C sheet mechanismsS P Bottomley, P C Hopkins, J C Whisstock
Pageof 4