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The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin

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Standard

The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. / Kern, D; Drakenberg, T; Wikström, M; Forsén, S; Bang, H; Fischer, G.

I: FEBS letters, Bind 323, Nr. 3, 01.06.1993, s. 198-202.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Kern, D, Drakenberg, T, Wikström, M, Forsén, S, Bang, H & Fischer, G 1993, 'The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin', FEBS letters, bind 323, nr. 3, s. 198-202. https://doi.org/10.1016/0014-5793(93)81338-Z

APA

Kern, D., Drakenberg, T., Wikström, M., Forsén, S., Bang, H., & Fischer, G. (1993). The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. FEBS letters, 323(3), 198-202. https://doi.org/10.1016/0014-5793(93)81338-Z

Vancouver

Kern D, Drakenberg T, Wikström M, Forsén S, Bang H, Fischer G. The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. FEBS letters. 1993 jun 1;323(3):198-202. https://doi.org/10.1016/0014-5793(93)81338-Z

Author

Kern, D ; Drakenberg, T ; Wikström, M ; Forsén, S ; Bang, H ; Fischer, G. / The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. I: FEBS letters. 1993 ; Bind 323, Nr. 3. s. 198-202.

Bibtex

@article{b06bdf4aec2f4b70a1428b001a1d46ab,
title = "The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin",
abstract = "The cytosolic peptidyl-prolyl cis/trans isomerase cyclophilin from pig kidney can accelerate catalytically the cis/trans isomerization of prolyl peptide bonds. One- and two-dimensional 1H NMR spectroscopy was used to prove that the polypeptide hormone calcitonin is a substrate for cyclophilin. Isomerization of only one of the two prolyl peptide bonds is catalyzed significantly. The efficiency of catalysis was calculated by lineshape analysis and NOESY spectroscopy. Cyclosporin A completely blocks the effect of the enzyme on the conformational dynamics of the polypeptide.",
keywords = "Amino Acid Isomerases, Amino Acid Sequence, Calcium, Carrier Proteins, Cyclosporins, Humans, Isomerism, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Peptidylprolyl Isomerase, Protein Conformation, Thermodynamics",
author = "D Kern and T Drakenberg and M Wikstr{\"o}m and S Fors{\'e}n and H Bang and G Fischer",
year = "1993",
month = jun,
day = "1",
doi = "http://dx.doi.org/10.1016/0014-5793(93)81338-Z",
language = "English",
volume = "323",
pages = "198--202",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "3",

}

RIS

TY - JOUR

T1 - The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin

AU - Kern, D

AU - Drakenberg, T

AU - Wikström, M

AU - Forsén, S

AU - Bang, H

AU - Fischer, G

PY - 1993/6/1

Y1 - 1993/6/1

N2 - The cytosolic peptidyl-prolyl cis/trans isomerase cyclophilin from pig kidney can accelerate catalytically the cis/trans isomerization of prolyl peptide bonds. One- and two-dimensional 1H NMR spectroscopy was used to prove that the polypeptide hormone calcitonin is a substrate for cyclophilin. Isomerization of only one of the two prolyl peptide bonds is catalyzed significantly. The efficiency of catalysis was calculated by lineshape analysis and NOESY spectroscopy. Cyclosporin A completely blocks the effect of the enzyme on the conformational dynamics of the polypeptide.

AB - The cytosolic peptidyl-prolyl cis/trans isomerase cyclophilin from pig kidney can accelerate catalytically the cis/trans isomerization of prolyl peptide bonds. One- and two-dimensional 1H NMR spectroscopy was used to prove that the polypeptide hormone calcitonin is a substrate for cyclophilin. Isomerization of only one of the two prolyl peptide bonds is catalyzed significantly. The efficiency of catalysis was calculated by lineshape analysis and NOESY spectroscopy. Cyclosporin A completely blocks the effect of the enzyme on the conformational dynamics of the polypeptide.

KW - Amino Acid Isomerases

KW - Amino Acid Sequence

KW - Calcium

KW - Carrier Proteins

KW - Cyclosporins

KW - Humans

KW - Isomerism

KW - Magnetic Resonance Spectroscopy

KW - Molecular Sequence Data

KW - Peptidylprolyl Isomerase

KW - Protein Conformation

KW - Thermodynamics

U2 - http://dx.doi.org/10.1016/0014-5793(93)81338-Z

DO - http://dx.doi.org/10.1016/0014-5793(93)81338-Z

M3 - Journal article

C2 - 8500610

VL - 323

SP - 198

EP - 202

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 3

ER -

ID: 50166461