Polymer dynamics from synthetic to biological macromolecules

被引:0
|
作者
Richter, D. [1 ]
Niedzwiedz, K. [1 ]
Monkenbusch, M. [1 ]
Wischnewski, A. [1 ]
Biehl, R. [1 ]
Hoffmann, B. [2 ]
Merkel, R. [2 ]
机构
[1] Forschungszentrum Julich, Inst Festkorperforsch, Postfach 1913, D-52425 Julich, Germany
[2] Forschungszentrum Julich, Inst Bio & Nanosyst, Postfach 1913, D-52425 Julich, Germany
来源
COMPLEX SYSTEMS-BOOK 1 | 2008年 / 982卷
关键词
aggregate dynamics; alcohol dehydrogenase; dynamic miscibility; neutron spin echo; polyethyleneoxide; polymethylmetacrylate; random environment; random friction; Rouse model; solution structure; PROTEIN; MOTION;
D O I
暂无
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
High resolution neutron scattering together with a meticulous choice of the contrast conditions allows to access the large scale dynamics of soft materials including biological molecules in space and time. In this contribution we present two examples. One from the world of synthetic polymers, the other from biomolecules. First, we will address the peculiar dynamics of miscible polymer blends with very different component glass transition temperatures. Polymethylmetacrylate (PMMA), polyethyleneoxide (PEO) are perfectly miscible but exhibit a difference in the glass transition temperature by 200K. We present quasielastic neutron scattering investigations on the dynamics of the fast component in the range from angstroms to nanometers over a time frame of five orders of magnitude. All data may be consistently described in terms of a Rouse model with random friction, reflecting the random environment imposed by the nearly frozen PMMA matrix on the fast mobile PEO. In the second part we touch on some new developments relating to large scale internal dynamics of proteins by neutron spin echo. We will report results of some pioneering studies which show the feasibility of such experiments on large scale protein motion which will most likely initiate further studies in the future.
引用
收藏
页码:429 / +
页数:3
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