In Situ Dynamic Light Scattering Complementing Neutron Spin Echo Measurements on Protein Samples

被引：4

作者：

Balacescu, L. ^{[1
,2
]}

Voegl, F. ^{[1
]}

Staringer, S. ^{[1
]}

Ossovyi, V ^{[1
]}

Brandl, G. ^{[1
]}

Lumma, N. ^{[3
,4
]}

Feilbach, H. ^{[3
,4
]}

Holderer, O. ^{[1
]}

Pasini, S. ^{[1
]}

Stadler, A. ^{[3
,4
]}

Fitter, J. ^{[2
,5
]}

Schrader, T. E. ^{[1
]}

机构：

[1] Forschungszentrum Julich, Julich Ctr Neutron Sci, Heinz Maier Leibnitz Zentrum, D-85748 Garching, Germany

[2] Rhein Westfalische TH Aachen, Phys Inst, AG Biophys, D-52074 Aachen, Germany

[3] Forschungszentrum Julich, Julich Ctr Neutron Sci, D-52425 Julich, Germany

[4] Inst Complex Syst, D-52425 Julich, Germany

[5] Forschungszentrum Julich, Inst Complex Syst ICS 5, D-52425 Julich, Germany

来源：

JOURNAL OF SURFACE INVESTIGATION | 2020年 / 14卷 / SUPPL 1期

关键词：

biopolymers; spin echo spectroscopy; in situ dynamic light scattering; aggregation;

D O I：

10.1134/S1027451020070046

中图分类号：

O469 [凝聚态物理学];

学科分类号：

070205 ;

摘要：

Monitoring the state of the sample on the minute-time scale is crucial in case of sensitive soft matter or biological samples, given that neutron spin echo measurements take up to several days. Moreover, there is no method to interpret the normalized intermediate scattering function obtained by measuring the neutron spin echo if relevant sample properties change during measurement. Dynamic light scattering provides information on the diffusion constant of particles in solution (biological macromolecules, such as proteins, protein aggregates, polymer particles, etc.) with average hydrodynamic radii in a wide range from several nanometers up to several microns. This information can be obtained in a few minutes and it offers a good overview of the current sample state. Details on the novel in situ dynamic light scattering set-up with one fixed scattering angle and first results obtained on a molten globule state of apo-myoglobin are presented.

引用

页码：S185 / S189

页数：5

共 9 条

[1] Exploring internal protein dynamics by neutron spin echo spectroscopy [J].

Biehl, Ralf ;

Monkenbusch, Michael ;

Richter, Dieter .

SOFT MATTER, 2011, 7 (04) :1299-1307

[2]

Chu B., 1974, LASER LIGHT SCATTERI

[3]

Kelman Z., 2016, Isotope Labeling of Biomolecules-Applications, Vvol. 566

[4] An introduction to NMR-based approaches for measuring protein dynamics [J].

Kleckner, Ian R. ;

Foster, Mark P. .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2011, 1814 (08) :942-968

[5] Influence of the cross-linker content on adsorbed functionalised microgel coatings [J].

Kyrey, Tetyana ;

Witte, Judith ;

Pipich, Vitaliy ;

Feoktystov, Artem ;

Koutsioubas, Alexandros ;

Vezhlev, Egor ;

Frielinghaus, Henrich ;

von Klitzing, Regine ;

Wellert, Stefan ;

Holderer, Olaf .

POLYMER, 2019, 169 :29-35

[6] J-NSE-Phoenix, a neutron spin-echo spectrometer with optimized superconducting precession coils at the MLZ in Garching [J].

Pasini, S. ;

Holderer, O. ;

Kozielewski, T. ;

Richter, D. ;

Monkenbusch, M. .

REVIEW OF SCIENTIFIC INSTRUMENTS, 2019, 90 (04)

[7] CONTIN - A GENERAL-PURPOSE CONSTRAINED REGULARIZATION PROGRAM FOR INVERTING NOISY LINEAR ALGEBRAIC AND INTEGRAL-EQUATIONS [J].

PROVENCHER, SW .

COMPUTER PHYSICS COMMUNICATIONS, 1982, 27 (03) :229-242

[8] Neutron Spin Echo in Polymer Systems [J].

Richter, D ;

Monkenbusch, M ;

Arbe, A ;

Colmenero, J .

NEUTRON SPIN ECHO IN POLYMER SYSTEMS, 2005, 174 :1-221

[9] Probing the Dynamics and Interactions of Disordered Proteins with Single-Molecule Spectroscopy [J].

Schuler, Ben .

BIOPHYSICAL JOURNAL, 2019, 116 (03) :12A-12A

← 1 →