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F X Schmid

Showing results (51-60 of 150) with videos related to

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Nature Structural Biology|May 10, 2000
Two exposed amino acid residues confer thermostability on a cold shock proteinD Perl, U Mueller, U Heinemann, et al.
Protein Science : a Publication of the Protein Society|July 1, 1992
Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutationD A Schultz, F X Schmid, R L Baldwin
Protein Science : a Publication of the Protein Society|January 1, 1992
Stability, quaternary structure, and folding of internal, external, and core-glycosylated invertase from yeastG Kern, N Schülke, F X Schmid, et al.
Journal of Molecular Biology|September 8, 1995
Destabilization of a protein helix by electrostatic interactionsS Walter, B Hubner, U Hahn, et al.
The EMBO Journal|January 15, 1996
Preferential binding of an unfolded protein to DsbAC Frech, M Wunderlich, R Glockshuber, et al.
Biochemistry|March 27, 1990
Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactionsT Kiefhaber, R Quaas, U Hahn, et al.
Journal of Molecular Biology|March 29, 2000
Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock proteinU Mueller, D Perl, F X Schmid, et al.
Journal of Molecular Biology|January 8, 1999
A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopyJ Balbach, C Steegborn, T Schindler, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1979
Role of proline isomerization in folding of ribonuclease A at low temperaturesK H Cook, F X Schmid, R L Baldwin
Journal of Molecular Biology|September 20, 1986
Folding mechanism of porcine ribonucleaseR Grafl, K Lang, A Wrba, et al.
Pageof 15

Showing results (51-60 of 150) with videos related to

Sort By:
Pageof 15
Nature Structural Biology|May 10, 2000
Two exposed amino acid residues confer thermostability on a cold shock proteinD Perl, U Mueller, U Heinemann, et al.
Protein Science : a Publication of the Protein Society|July 1, 1992
Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutationD A Schultz, F X Schmid, R L Baldwin
Protein Science : a Publication of the Protein Society|January 1, 1992
Stability, quaternary structure, and folding of internal, external, and core-glycosylated invertase from yeastG Kern, N Schülke, F X Schmid, et al.
Journal of Molecular Biology|September 8, 1995
Destabilization of a protein helix by electrostatic interactionsS Walter, B Hubner, U Hahn, et al.
The EMBO Journal|January 15, 1996
Preferential binding of an unfolded protein to DsbAC Frech, M Wunderlich, R Glockshuber, et al.
Biochemistry|March 27, 1990
Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactionsT Kiefhaber, R Quaas, U Hahn, et al.
Journal of Molecular Biology|March 29, 2000
Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock proteinU Mueller, D Perl, F X Schmid, et al.
Journal of Molecular Biology|January 8, 1999
A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopyJ Balbach, C Steegborn, T Schindler, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1979
Role of proline isomerization in folding of ribonuclease A at low temperaturesK H Cook, F X Schmid, R L Baldwin
Journal of Molecular Biology|September 20, 1986
Folding mechanism of porcine ribonucleaseR Grafl, K Lang, A Wrba, et al.
Pageof 15