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F X Schmid

Showing results (21-30 of 150) with videos related to

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Biochemistry|March 6, 1990
The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cellG Fischer, F X Schmid
Journal of Molecular Biology|March 5, 1992
Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1T Kiefhaber, F X Schmid
Journal of Molecular Biology|March 5, 1990
Role of two proline-containing turns in the folding of porcine ribonucleaseK Lang, F X Schmid
Nature|February 4, 1988
Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein foldingK Lang, F X Schmid
Biochemistry|March 30, 1982
Fast- and slow-refolding forms of unfolded ribonuclease A differ in tyrosine fluorescenceA Rehage, F X Schmid
Journal of Molecular Biology|August 4, 1995
Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1C Frech, F X Schmid
Biochemistry|December 6, 1994
Folding mechanism of ribonuclease T1 in the absence of the disulfide bondsM Mücke, F X Schmid
The Journal of Biological Chemistry|June 25, 1988
The stability of yeast invertase is not significantly influenced by glycosylationN Schülke, F X Schmid
Journal of Molecular Biology|November 25, 1979
Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchangeF X Schmid, R L Baldwin
Biochemistry|August 10, 1993
Stabilization of a protein by guanidinium chlorideL M Mayr, F X Schmid
Pageof 15

Showing results (21-30 of 150) with videos related to

Sort By:
Pageof 15
Biochemistry|March 6, 1990
The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cellG Fischer, F X Schmid
Journal of Molecular Biology|March 5, 1992
Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1T Kiefhaber, F X Schmid
Journal of Molecular Biology|March 5, 1990
Role of two proline-containing turns in the folding of porcine ribonucleaseK Lang, F X Schmid
Nature|February 4, 1988
Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein foldingK Lang, F X Schmid
Biochemistry|March 30, 1982
Fast- and slow-refolding forms of unfolded ribonuclease A differ in tyrosine fluorescenceA Rehage, F X Schmid
Journal of Molecular Biology|August 4, 1995
Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1C Frech, F X Schmid
Biochemistry|December 6, 1994
Folding mechanism of ribonuclease T1 in the absence of the disulfide bondsM Mücke, F X Schmid
The Journal of Biological Chemistry|June 25, 1988
The stability of yeast invertase is not significantly influenced by glycosylationN Schülke, F X Schmid
Journal of Molecular Biology|November 25, 1979
Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchangeF X Schmid, R L Baldwin
Biochemistry|August 10, 1993
Stabilization of a protein by guanidinium chlorideL M Mayr, F X Schmid
Pageof 15