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O Bilsel

Showing results (1-10 of 5) with videos related to

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Protein Science : a Publication of the Protein Society|August 19, 1999
The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coliP J Gualfetti, O Bilsel, C R Matthews
Biochemistry|January 20, 1999
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channelsO Bilsel, J A Zitzewitz, K E Bowers, et al.
Biochemistry|April 9, 1999
Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation timeO Bilsel, L Yang, J A Zitzewitz, et al.
Biochemistry|October 3, 1995
Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopyJ A Zitzewitz, O Bilsel, J Luo, et al.
Biochemistry|October 21, 1999
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel proteinP J Gualfetti, M Iwakura, J C Lee, et al.
Pageof 1

Showing results (1-10 of 5) with videos related to

Sort By:
Pageof 1
Protein Science : a Publication of the Protein Society|August 19, 1999
The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coliP J Gualfetti, O Bilsel, C R Matthews
Biochemistry|January 20, 1999
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channelsO Bilsel, J A Zitzewitz, K E Bowers, et al.
Biochemistry|April 9, 1999
Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation timeO Bilsel, L Yang, J A Zitzewitz, et al.
Biochemistry|October 3, 1995
Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopyJ A Zitzewitz, O Bilsel, J Luo, et al.
Biochemistry|October 21, 1999
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel proteinP J Gualfetti, M Iwakura, J C Lee, et al.
Pageof 1