Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP

K Teilum; B B Kragelund; J Knudsen; F M Poulsen

doi:10.1006/jmbi.2000.4003

Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP

K Teilum, B B Kragelund, J Knudsen, F M Poulsen

Biomolecular Sciences

29 Citations (Scopus)

Abstract

A burst phase in the early folding of the four-helix two-state folder protein acyl-coenzyme A binding protein (ACBP) has been detected using quenched-flow in combination with site-specific NMR-detected hydrogen exchange. Several of the burst phase structures coincide with a structure consisting of eight conserved hydrophobic residues at the interface between the two N and C-terminal helices. Previous mutation studies have shown that the formation of this structure is rate limiting for the final folding of ACBP. The burst phase structures observed in ACBP are different from the previously reported collapsed types of burst phase intermediates observed in the folding of other proteins.

Original language	English
Journal	Journal of Molecular Biology
Volume	301
Issue number	5
Pages (from-to)	1307-14
Number of pages	7
ISSN	0022-2836
DOIs	https://doi.org/10.1006/jmbi.2000.4003
Publication status	Published - 2000

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title = "Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP",

abstract = "A burst phase in the early folding of the four-helix two-state folder protein acyl-coenzyme A binding protein (ACBP) has been detected using quenched-flow in combination with site-specific NMR-detected hydrogen exchange. Several of the burst phase structures coincide with a structure consisting of eight conserved hydrophobic residues at the interface between the two N and C-terminal helices. Previous mutation studies have shown that the formation of this structure is rate limiting for the final folding of ACBP. The burst phase structures observed in ACBP are different from the previously reported collapsed types of burst phase intermediates observed in the folding of other proteins.",

author = "K Teilum and Kragelund, {B B} and J Knudsen and Poulsen, {F M}",

note = "Keywords: Amides; Animals; Carrier Proteins; Cattle; Conserved Sequence; Diazepam Binding Inhibitor; Hydrogen; Hydrogen Bonding; Hydrogen-Ion Concentration; Isoleucine; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Protein Folding; Protein Structure, Secondary; Protons; Serine",

year = "2000",

doi = "10.1006/jmbi.2000.4003",

language = "English",

volume = "301",

pages = "1307--14",

journal = "Journal of Molecular Biology",

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T1 - Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP

AU - Teilum, K

AU - Kragelund, B B

AU - Knudsen, J

AU - Poulsen, F M

N1 - Keywords: Amides; Animals; Carrier Proteins; Cattle; Conserved Sequence; Diazepam Binding Inhibitor; Hydrogen; Hydrogen Bonding; Hydrogen-Ion Concentration; Isoleucine; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Protein Folding; Protein Structure, Secondary; Protons; Serine

PY - 2000

Y1 - 2000

N2 - A burst phase in the early folding of the four-helix two-state folder protein acyl-coenzyme A binding protein (ACBP) has been detected using quenched-flow in combination with site-specific NMR-detected hydrogen exchange. Several of the burst phase structures coincide with a structure consisting of eight conserved hydrophobic residues at the interface between the two N and C-terminal helices. Previous mutation studies have shown that the formation of this structure is rate limiting for the final folding of ACBP. The burst phase structures observed in ACBP are different from the previously reported collapsed types of burst phase intermediates observed in the folding of other proteins.

AB - A burst phase in the early folding of the four-helix two-state folder protein acyl-coenzyme A binding protein (ACBP) has been detected using quenched-flow in combination with site-specific NMR-detected hydrogen exchange. Several of the burst phase structures coincide with a structure consisting of eight conserved hydrophobic residues at the interface between the two N and C-terminal helices. Previous mutation studies have shown that the formation of this structure is rate limiting for the final folding of ACBP. The burst phase structures observed in ACBP are different from the previously reported collapsed types of burst phase intermediates observed in the folding of other proteins.

U2 - 10.1006/jmbi.2000.4003

DO - 10.1006/jmbi.2000.4003

M3 - Journal article

C2 - 10966822

SN - 0022-2836

VL - 301

SP - 1307

EP - 1314

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 5

ER -

Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP

Abstract

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