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S G Burston

Showing results (1-10 of 16) with videos related to

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Essays in Biochemistry|January 1, 1995
Molecular chaperones: physical and mechanistic propertiesS G Burston, A R Clarke
Journal of Molecular Biology|May 26, 1995
The origins and consequences of asymmetry in the chaperonin reaction cycleS G Burston, N A Ranson, A R Clarke
Journal of Molecular Biology|March 7, 1997
Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reactionN A Ranson, S G Burston, A R Clarke
The Biochemical Journal|June 15, 1994
Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10R A Staniforth, S G Burston, T Atkinson, et al.
Journal of Molecular Biology|July 28, 1995
Chaperonins can catalyse the reversal of early aggregation steps when a protein misfoldsN A Ranson, N J Dunster, S G Burston, et al.
Methods in Enzymology|April 16, 1998
Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroELA L Horwich, S G Burston, H S Rye, et al.
Nature|September 5, 1996
Release of both native and non-native proteins from a cis-only GroEL ternary complexS G Burston, J S Weissman, G W Farr, et al.
FEBS Letters|May 16, 1994
The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted foldingR A Staniforth, A Cortés, S G Burston, et al.
Annals of the New York Academy of Sciences|November 30, 1992
The influence of chaperonins on protein folding. A mechanism for increasing the yield of the native formS G Burston, R Sleigh, D J Halsall, et al.
Annual Review of Biochemistry|October 6, 1998
Structure and function in GroEL-mediated protein foldingP B Sigler, Z Xu, H S Rye, et al.
Pageof 2

Showing results (1-10 of 16) with videos related to

Sort By:
Pageof 2
Essays in Biochemistry|January 1, 1995
Molecular chaperones: physical and mechanistic propertiesS G Burston, A R Clarke
Journal of Molecular Biology|May 26, 1995
The origins and consequences of asymmetry in the chaperonin reaction cycleS G Burston, N A Ranson, A R Clarke
Journal of Molecular Biology|March 7, 1997
Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reactionN A Ranson, S G Burston, A R Clarke
The Biochemical Journal|June 15, 1994
Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10R A Staniforth, S G Burston, T Atkinson, et al.
Journal of Molecular Biology|July 28, 1995
Chaperonins can catalyse the reversal of early aggregation steps when a protein misfoldsN A Ranson, N J Dunster, S G Burston, et al.
Methods in Enzymology|April 16, 1998
Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroELA L Horwich, S G Burston, H S Rye, et al.
Nature|September 5, 1996
Release of both native and non-native proteins from a cis-only GroEL ternary complexS G Burston, J S Weissman, G W Farr, et al.
FEBS Letters|May 16, 1994
The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted foldingR A Staniforth, A Cortés, S G Burston, et al.
Annals of the New York Academy of Sciences|November 30, 1992
The influence of chaperonins on protein folding. A mechanism for increasing the yield of the native formS G Burston, R Sleigh, D J Halsall, et al.
Annual Review of Biochemistry|October 6, 1998
Structure and function in GroEL-mediated protein foldingP B Sigler, Z Xu, H S Rye, et al.
Pageof 2