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

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Standard

Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP. / Teilum, K; Kragelund, B B; Knudsen, J; Poulsen, F M.

I: Journal of Molecular Biology, Bind 301, Nr. 5, 2000, s. 1307-14.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Teilum, K, Kragelund, BB, Knudsen, J & Poulsen, FM 2000, 'Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP', Journal of Molecular Biology, bind 301, nr. 5, s. 1307-14. https://doi.org/10.1006/jmbi.2000.4003

APA

Teilum, K., Kragelund, B. B., Knudsen, J., & Poulsen, F. M. (2000). Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP. Journal of Molecular Biology, 301(5), 1307-14. https://doi.org/10.1006/jmbi.2000.4003

Vancouver

Teilum K, Kragelund BB, Knudsen J, Poulsen FM. Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP. Journal of Molecular Biology. 2000;301(5):1307-14. https://doi.org/10.1006/jmbi.2000.4003

Author

Teilum, K ; Kragelund, B B ; Knudsen, J ; Poulsen, F M. / Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP. I: Journal of Molecular Biology. 2000 ; Bind 301, Nr. 5. s. 1307-14.

Bibtex

@article{c7a7adb0b98811df825b000ea68e967b,
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",
issn = "0022-2836",
publisher = "Academic Press",
number = "5",

}

RIS

TY - JOUR

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

VL - 301

SP - 1307

EP - 1314

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 5

ER -

ID: 21833041