Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements

被引：39

作者：

Baldwin, Andrew J. ^{[1
]}

Anthony-Cahill, Spencer J. ^{[1
]}

Knowles, Tuomas P. J. ^{[2
]}

Lippens, Guy ^{[3
,4
]}

Christodoulou, John ^{[1
]}

Barker, Paul D. ^{[1
]}

Dobson, Christopher M. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

[2] Univ Cambridge, Ctr Nanosci, Cambridge CB3 0FF, England

[3] Univ Cambridge, Cavendish Lab, Cambridge CB3 0FF, England

[4] CNRS, UMR 8576, F-59655 Villeneuve Dascq, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 18期

基金：

英国惠康基金;

关键词：

amyloid fibrils; diffusion; NMR spectroscopy; rotational motion;

D O I：

10.1002/anie.200703915

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented). Telling fibrils: Diffusion data obtained by solution NMR spectroscopy from flexible regions of amyloid fibrils for both rotational and translation diffusion combined is of similar magnitude to that measured using AFM and TEM (see picture). Fibrils in solution are calculated to be somewhat longer on average than those deposited on surfaces for microscopy experiments, which can be partially attributed to the sensitivity of fibrils to fracture. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：3385 / 3387

页数：3

共 14 条

[1] Cytochrome display on amyloid fibrils [J].

Baldwin, AJ ;

Bader, R ;

Christodoulou, J ;

MacPhee, CE ;

Dobson, CM ;

Barker, PD .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (07) :2162-2163

[2] Contribution of rotational diffusion to pulsed field gradient diffusion measurements [J].

Baldwin, Andrew J. ;

Christodoulou, John ;

Barker, Paul D. ;

Dobson, Christopher M. ;

Lippens, Guy .

JOURNAL OF CHEMICAL PHYSICS, 2007, 127 (11)

[3] Molecular recycling within amyloid fibrils [J].

Carulla, N ;

Caddy, GL ;

Hall, DR ;

Zurdo, J ;

Gairí, M ;

Feliz, M ;

Giralt, E ;

Robinson, CV ;

Dobson, CM .

NATURE, 2005, 436 (7050) :554-558

[4] IDENTIFICATION BY H-1-NMR SPECTROSCOPY OF FLEXIBLE C-TERMINAL EXTENSIONS IN BOVINE LENS ALPHA-CRYSTALLIN [J].

CARVER, JA ;

AQUILINA, JA ;

TRUSCOTT, RJW ;

RALSTON, GB .

FEBS LETTERS, 1992, 311 (02) :143-149

[5] Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes [J].

Christodoulou, J ;

Larsson, G ;

Fucini, P ;

Connell, SR ;

Pertinhez, TA ;

Hanson, CL ;

Redfield, C ;

Nierhaus, KH ;

Robinson, CV ;

Schleucher, J ;

Dobson, CM .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (30) :10949-10954

[6] Diffusion NMR spectroscopy: Folding and aggregation of domains in p53 [J].

Dehner, A ;

Kessler, H .

CHEMBIOCHEM, 2005, 6 (09) :1550-1565

[7] RAPID ESTIMATION OF LENGTH DISTRIBUTIONS OF MICROTUBULE PREPARATIONS BY QUASI-ELASTIC LIGHT-SCATTERING [J].

HALLETT, FR ;

KEATES, R .

BIOPOLYMERS, 1985, 24 (12) :2403-2415

[8] Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human αA-, αβ- and R120G αB-Crystallins [J].

Meehan, Sarah ;

Knowles, Tuomas P. J. ;

Baldwin, Andrew J. ;

Smith, Jeffrey F. ;

Squires, Adam M. ;

clements, Phillip ;

Treweek, Teresa M. ;

Ecroyd, Heath ;

Tartaglia, Gian Gaetano ;

Vendruscolo, Michele ;

MacPhee, Cait E. ;

Dobson, Christopher M. ;

Carver, John A. .

JOURNAL OF MOLECULAR BIOLOGY, 2007, 372 (02) :470-484

[9] Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome [J].

Mulder, FAA ;

Bouakaz, L ;

Lundell, A ;

Venkataramana, M ;

Liljas, A ;

Akke, M ;

Sanyal, S .

BIOCHEMISTRY, 2004, 43 (20) :5930-5936

[10] DYNAMICS OF THE MULTIDOMAIN FIBRINOLYTIC PROTEIN UROKINASE FROM TWO-DIMENSIONAL NMR [J].

OSWALD, RE ;

BOGUSKY, MJ ;

BAMBERGER, M ;

SMITH, RAG ;

DOBSON, CM .

NATURE, 1989, 337 (6207) :579-582

← 1 2 →