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W A Houry

Showing results (1-10 of 12) with videos related to

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Current Protein & Peptide Science|October 9, 2002
Chaperone-assisted protein folding in the cell cytoplasmW A Houry
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire|November 22, 2001
Mechanism of substrate recognition by the chaperonin GroELW A Houry
Biochemistry|September 10, 1996
Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchangeW A Houry, H A Scheraga
Biochemistry|September 10, 1996
Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerizationW A Houry, H A Scheraga
Nature Structural Biology|June 1, 1995
The nature of the initial step in the conformational folding of disulphide-intact ribonuclease AW A Houry, D M Rothwarf, H A Scheraga
Biochemistry|August 6, 1996
Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease AW A Houry, D M Rothwarf, H A Scheraga
Biochemistry|March 8, 1994
A very fast phase in the refolding of disulfide-intact ribonuclease A: implications for the refolding and unfolding pathwaysW A Houry, D M Rothwarf, H A Scheraga
Proceedings of the National Academy of Sciences of the United States of America|May 16, 1998
Definition of amide protection factors for early kinetic intermediates in protein foldingW A Houry, J M Sauder, H Roder, et al.
Nature|January 26, 2000
Identification of in vivo substrates of the chaperonin GroELW A Houry, D Frishman, C Eckerskorn, et al.
Cell|August 8, 1997
In vivo observation of polypeptide flux through the bacterial chaperonin systemK L Ewalt, J P Hendrick, W A Houry, et al.
Pageof 2

Showing results (1-10 of 12) with videos related to

Sort By:
Pageof 2
Current Protein & Peptide Science|October 9, 2002
Chaperone-assisted protein folding in the cell cytoplasmW A Houry
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire|November 22, 2001
Mechanism of substrate recognition by the chaperonin GroELW A Houry
Biochemistry|September 10, 1996
Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchangeW A Houry, H A Scheraga
Biochemistry|September 10, 1996
Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerizationW A Houry, H A Scheraga
Nature Structural Biology|June 1, 1995
The nature of the initial step in the conformational folding of disulphide-intact ribonuclease AW A Houry, D M Rothwarf, H A Scheraga
Biochemistry|August 6, 1996
Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease AW A Houry, D M Rothwarf, H A Scheraga
Biochemistry|March 8, 1994
A very fast phase in the refolding of disulfide-intact ribonuclease A: implications for the refolding and unfolding pathwaysW A Houry, D M Rothwarf, H A Scheraga
Proceedings of the National Academy of Sciences of the United States of America|May 16, 1998
Definition of amide protection factors for early kinetic intermediates in protein foldingW A Houry, J M Sauder, H Roder, et al.
Nature|January 26, 2000
Identification of in vivo substrates of the chaperonin GroELW A Houry, D Frishman, C Eckerskorn, et al.
Cell|August 8, 1997
In vivo observation of polypeptide flux through the bacterial chaperonin systemK L Ewalt, J P Hendrick, W A Houry, et al.
Pageof 2