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L L Randall

Showing results (51-60 of 71) with videos related to

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European Journal of Biochemistry|December 1, 1978
Processing in vitro of precursor periplasmic proteins from Escherichia coliL L Randall, L G Josefsson, S J Hardy
The Journal of Biological Chemistry|October 5, 1993
Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitroS Y Chun, S Strobel, P Bassford, et al.
Protein Science : a Publication of the Protein Society|June 1, 1995
Interaction of SecB with intermediates along the folding pathway of maltose-binding proteinD L Diamond, S Strobel, S Y Chun, et al.
Protein Science : a Publication of the Protein Society|May 30, 1998
Calorimetric analyses of the interaction between SecB and its ligandsL L Randall, T B Topping, D Suciu, et al.
The Journal of Biological Chemistry|October 15, 1988
Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported proteinG P Liu, T B Topping, W H Cover, et al.
Protein Science : a Publication of the Protein Society|March 1, 1996
Electrospray mass spectrometric investigation of the chaperone SecBV F Smith, B L Schwartz, L L Randall, et al.
American Indian and Alaska Native Mental Health Research (Online)|August 3, 2001
The Aberdeen Indian Health Service infant mortality study: design, methodology, and implementationL L Randall, C Krogh, T K Welty, et al.
Science (New York, N.Y.)|February 26, 1988
Modulation of folding pathways of exported proteins by the leader sequenceS Park, G Liu, T B Topping, et al.
The Journal of Biological Chemistry|June 26, 1999
Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimersE M Murén, D Suciu, T B Topping, et al.
The Journal of Biological Chemistry|June 25, 1991
Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coliC M Teschke, J Kim, T Song, et al.
Pageof 8

Showing results (51-60 of 71) with videos related to

Sort By:
Pageof 8
European Journal of Biochemistry|December 1, 1978
Processing in vitro of precursor periplasmic proteins from Escherichia coliL L Randall, L G Josefsson, S J Hardy
The Journal of Biological Chemistry|October 5, 1993
Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitroS Y Chun, S Strobel, P Bassford, et al.
Protein Science : a Publication of the Protein Society|June 1, 1995
Interaction of SecB with intermediates along the folding pathway of maltose-binding proteinD L Diamond, S Strobel, S Y Chun, et al.
Protein Science : a Publication of the Protein Society|May 30, 1998
Calorimetric analyses of the interaction between SecB and its ligandsL L Randall, T B Topping, D Suciu, et al.
The Journal of Biological Chemistry|October 15, 1988
Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported proteinG P Liu, T B Topping, W H Cover, et al.
Protein Science : a Publication of the Protein Society|March 1, 1996
Electrospray mass spectrometric investigation of the chaperone SecBV F Smith, B L Schwartz, L L Randall, et al.
American Indian and Alaska Native Mental Health Research (Online)|August 3, 2001
The Aberdeen Indian Health Service infant mortality study: design, methodology, and implementationL L Randall, C Krogh, T K Welty, et al.
Science (New York, N.Y.)|February 26, 1988
Modulation of folding pathways of exported proteins by the leader sequenceS Park, G Liu, T B Topping, et al.
The Journal of Biological Chemistry|June 26, 1999
Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimersE M Murén, D Suciu, T B Topping, et al.
The Journal of Biological Chemistry|June 25, 1991
Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coliC M Teschke, J Kim, T Song, et al.
Pageof 8