TY  - JOUR
AU  - Grimaldo, Marco
AU  - Roosen-Runge, Felix
AU  - Hennig, Marcus
AU  - Zanini, Fabio
AU  - Zhang, Fajun
AU  - Jalarvo, Niina
AU  - Zamponi, Michaela
AU  - Schreiber, Frank
AU  - Seydel, Tilo
TI  - Hierarchical molecular dynamics of bovine serum albumin in concentrated aqueous solution below and above thermal denaturation
JO  - Physical chemistry, chemical physics
VL  - 17
IS  - 6
SN  - 1463-9084
CY  - Cambridge
PB  - RSC Publ.
M1  - FZJ-2015-01087
SP  - 4645 - 4655
PY  - 2015
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000349005900077
C6  - pmid:25587698
DO  - DOI:10.1039/C4CP04944F
UR  - https://juser.fz-juelich.de/record/187418
ER  -