The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP

Birthe Brandt Kragelund; Peter Osmark; Thomas B. Neergaard; Jacob Schiødt; Karsten Kristiansen; Jens Knudsen; Flemming Poulsen

doi:10.1038/9384

The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP

Birthe Brandt Kragelund, Peter Osmark, Thomas B. Neergaard, Jacob Schiødt, Karsten Kristiansen, Jens Knudsen, Flemming Poulsen

Biomolecular Sciences

134 Citations (Scopus)

Abstract

The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction.

Original language	English
Journal	Nature Structural and Molecular Biology
Volume	6
Issue number	6
Pages (from-to)	594-601
ISSN	1545-9993
DOIs	https://doi.org/10.1038/9384
Publication status	Published - 1999

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The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. / Kragelund, Birthe Brandt; Osmark, Peter; Neergaard, Thomas B. et al.

In: Nature Structural and Molecular Biology, Vol. 6, No. 6, 1999, p. 594-601.

Research output: Contribution to journal › Journal article › Research › peer-review

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abstract = "The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction.",

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T1 - The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP

AU - Kragelund, Birthe Brandt

AU - Osmark, Peter

AU - Neergaard, Thomas B.

AU - Schiødt, Jacob

AU - Kristiansen, Karsten

AU - Knudsen, Jens

AU - Poulsen, Flemming

PY - 1999

Y1 - 1999

N2 - The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction.

AB - The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction.

U2 - 10.1038/9384

DO - 10.1038/9384

M3 - Journal article

SN - 1545-9993

VL - 6

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EP - 601

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 6

ER -

The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP

Abstract

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