Photocontrolled folding and unfolding of a collagen triple helix

被引：92

作者：

Kusebauch, Ulrike

Cadamuro, Sergio A.

Musiol, Hans-Juergen

Lenz, Martin O.

Wachtveitl, Josef

Moroder, Luis

Renner, Christian

机构：

[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany

[2] Goethe Univ Frankfurt, Inst Phys & Theoret Chem, D-60438 Frankfurt, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 42期

关键词：

collagen; folding/unfolding; peptides; photoswitches; triple helix;

D O I：

10.1002/anie.200601432

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) At the flick of a switch: Two side chains of a collagen peptide containing (2S,4S)-mercaptoproline at two defined positions are linked with a diiodo azobenzene derivative. With the trans isomer of the azobenzene clamp (orange), the peptide folds into the collagen triple helix (green, blue, gray), which unfolds upon irradiation at 330 nm. The light-controlled folding/unfolding processes are fully reversible, making this system well-suited for ultrafast spectroscopic analysis. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.

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页码：7015 / 7018

页数：4

相关论文

共 43 条

[1] FOLDING MECHANISM OF THE TRIPLE HELIX IN TYPE-III COLAGEN AND TYPE-III PN-COLLAGEN - ROLE OF DISULFIDE BRIDGES AND PEPTIDE-BOND ISOMERIZATION [J].

BACHINGER, HP ;

BRUCKNER, P ;

TIMPL, R ;

PROCKOP, DJ ;

ENGEL, J .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1980, 106 (02) :619-632

[2] Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier [J].

Bachmann, A ;

Kiefhaber, T ;

Boudko, S ;

Engel, J ;

Bächinger, HP .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (39) :13897-13902

[3]

Bächinger HP, 2005, PROTEIN FOLDING HANDBOOK, P1059

[4] The role of cystine knots in collagen folding and stability, part II.: Conformational properties of (Pro-Hyp-Gly)n model trimers with N- and C-terminal collagen type III cystine knots [J].

Barth, D ;

Kyrieleis, O ;

Frank, S ;

Renner, C ;

Moroder, L .

CHEMISTRY-A EUROPEAN JOURNAL, 2003, 9 (15) :3703-3714

[5] Supercoiled protein motifs:: The collagen triple-helix and the α-helical coiled coil [J].

Beck, K ;

Brodsky, B .

JOURNAL OF STRUCTURAL BIOLOGY, 1998, 122 (1-2) :17-29

[6] HYDRATION STRUCTURE OF A COLLAGEN PEPTIDE [J].

BELLA, J ;

BRODSKY, B ;

BERMAN, HM .

STRUCTURE, 1995, 3 (09) :893-906

[7] CRYSTAL-STRUCTURE AND MOLECULAR-STRUCTURE OF A COLLAGEN-LIKE PEPTIDE AT 1.9-ANGSTROM RESOLUTION [J].

BELLA, J ;

EATON, M ;

BRODSKY, B ;

BERMAN, HM .

SCIENCE, 1994, 266 (5182) :75-81

[8] Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 [J].

Berisio, R ;

Vitagliano, L ;

Mazzarella, L ;

Zagari, A .

PROTEIN SCIENCE, 2002, 11 (02) :262-270

[9] Structure formation in the C terminus of type III collagen guides disulfide cross-linking [J].

Boudko, SP ;

Engel, J .

JOURNAL OF MOLECULAR BIOLOGY, 2004, 335 (05) :1289-1297

[10] Picosecond conformational transition and equilibration of a cyclic peptide [J].

Bredenbeck, J ;

Helbing, J ;

Sieg, A ;

Schrader, T ;

Zinth, W ;

Renner, C ;

Behrendt, R ;

Moroder, L ;

Wachtveitl, J ;

Hamm, P .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (11) :6452-6457

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