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J P Waltho

Showing results (11-20 of 39) with videos related to

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Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signalH C Shin, G Merutka, J P Waltho, et al.
Proteins|July 9, 1999
Differences in the effects of TFE on the folding pathways of human stefins A and BE Zerovnik, R Virden, R Jerala, et al.
Nature Structural Biology|September 1, 1995
Calcium-induced structural changes and domain autonomy in calmodulinB E Finn, J Evenäs, T Drakenberg, et al.
The Journal of Biological Chemistry|March 17, 1995
Characterization of the Elk-1 ETS DNA-binding domainP Shore, L Bisset, J Lakey, et al.
Proteins|August 26, 1998
On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate statesE Zerovnik, R Jerala, R Virden, et al.
Journal of Molecular Biology|August 5, 1992
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. MyohemerythrinH J Dyson, G Merutka, J P Waltho, et al.
Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobinJ P Waltho, V A Feher, G Merutka, et al.
European Journal of Biochemistry|November 1, 1994
Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinasesJ R Martin, R Jerala, L Kroon-Zitko, et al.
Nature Structural Biology|March 21, 1998
Topology, sequence evolution and folding dynamics of an immunoglobulin domainM J Parker, C E Dempsey, L L Hosszu, et al.
Biochemistry|June 4, 1998
The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin LS Estrada, M Nycander, N J Hill, et al.
Pageof 4

Showing results (11-20 of 39) with videos related to

Sort By:
Pageof 4
Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signalH C Shin, G Merutka, J P Waltho, et al.
Proteins|July 9, 1999
Differences in the effects of TFE on the folding pathways of human stefins A and BE Zerovnik, R Virden, R Jerala, et al.
Nature Structural Biology|September 1, 1995
Calcium-induced structural changes and domain autonomy in calmodulinB E Finn, J Evenäs, T Drakenberg, et al.
The Journal of Biological Chemistry|March 17, 1995
Characterization of the Elk-1 ETS DNA-binding domainP Shore, L Bisset, J Lakey, et al.
Proteins|August 26, 1998
On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate statesE Zerovnik, R Jerala, R Virden, et al.
Journal of Molecular Biology|August 5, 1992
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. MyohemerythrinH J Dyson, G Merutka, J P Waltho, et al.
Biochemistry|June 29, 1993
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobinJ P Waltho, V A Feher, G Merutka, et al.
European Journal of Biochemistry|November 1, 1994
Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinasesJ R Martin, R Jerala, L Kroon-Zitko, et al.
Nature Structural Biology|March 21, 1998
Topology, sequence evolution and folding dynamics of an immunoglobulin domainM J Parker, C E Dempsey, L L Hosszu, et al.
Biochemistry|June 4, 1998
The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin LS Estrada, M Nycander, N J Hill, et al.
Pageof 4