Description: Hierarchical molecular dynamics of bovine serum albumin in concentrated aqueous solution below and above thermal denaturation

This title appears in the Scientific Report : 2015

Hierarchical molecular dynamics of bovine serum albumin in concentrated aqueous solution below and above thermal denaturation

The dynamics of proteins in solution is a complex and hierarchical process, affected by the aqueous environment as well as temperature. We present a comprehensive study on nanosecond time and nanometer length scales below, at, and above the denaturation temperature Td. Our experimental data evidence...

Personal Name(s):	Grimaldo, Marco (Corresponding Author)
	Roosen-Runge, Felix / Hennig, Marcus / Zanini, Fabio / Zhang, Fajun / Jalarvo, Niina / Zamponi, Michaela / Schreiber, Frank / Seydel, Tilo
Contributing Institute:	Neutronenstreuung; ICS-1 JCNS-FRM-II; JCNS-FRM-II JCNS-SNS; JCNS-SNS Neutronenstreuung; JCNS-1
Published in:	Physical chemistry, chemical physics, 17 (2015) 6, S. 4645 - 4655
Imprint:	Cambridge RSC Publ. 2015
DOI:	10.1039/C4CP04944F
PubMed ID:	25587698
Document Type:	Journal Article
Research Program:	Soft Matter, Health and Life Sciences Jülich Centre for Neutron Research (JCNS) Functional Macromolecules and Complexes
Subject (ZB):	Soft Condensed Matter > 0 Health and Life > 1 Health and Life > 0
Link:	OpenAccess
	Publikationsportal JuSER

Please use the identifier: http://hdl.handle.net/2128/8329 in citations.
Please use the identifier: http://dx.doi.org/10.1039/C4CP04944F in citations.

The dynamics of proteins in solution is a complex and hierarchical process, affected by the aqueous environment as well as temperature. We present a comprehensive study on nanosecond time and nanometer length scales below, at, and above the denaturation temperature Td. Our experimental data evidence dynamical processes in protein solutions on three distinct time scales. We suggest a consistent physical picture of hierarchical protein dynamics: (i) self-diffusion of the entire protein molecule is confirmed to agree with colloid theory for all temperatures where the protein is in its native conformational state. At higher temperatures T > Td, the self-diffusion is strongly obstructed by cross-linking or entanglement. (ii) The amplitude of backbone fluctuations grows with increasing T, and a transition in its dynamics is observed above Td. (iii) The number of mobile side-chains increases sharply at Td while their average dynamics exhibits only little variations. The combination of quasi-elastic neutron scattering and the presented analytical framework provides a detailed microscopic picture of the protein molecular dynamics in solution, thereby reflecting the changes of macroscopic properties such as cluster formation and gelation.