Hierarchical molecular dynamics of bovine serum albumin in concentrated aqueous solution below and above thermal denaturation
(2015) In Physical Chemistry Chemical Physics 17(6). p.4645-4655- Abstract
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... (More)
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. This journal is
(Less)
- author
- Grimaldo, Marco ; Roosen-Runge, Felix LU ; Hennig, Marcus ; Zanini, Fabio ; Zhang, Fajun ; Jalarvo, Niina ; Zamponi, Michaela ; Schreiber, Frank and Seydel, Tilo
- publishing date
- 2015-02-14
- type
- Contribution to journal
- publication status
- published
- in
- Physical Chemistry Chemical Physics
- volume
- 17
- issue
- 6
- pages
- 11 pages
- publisher
- Royal Society of Chemistry
- external identifiers
-
- pmid:25587698
- scopus:84964262070
- ISSN
- 1463-9076
- DOI
- 10.1039/c4cp04944f
- language
- English
- LU publication?
- no
- id
- 8f6fdbaf-338f-4a01-bc66-4904d6800b73
- date added to LUP
- 2018-12-17 09:41:47
- date last changed
- 2024-10-01 12:43:05
@article{8f6fdbaf-338f-4a01-bc66-4904d6800b73, abstract = {{<p>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 T<sub>d</sub>. 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 > T<sub>d</sub>, 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 T<sub>d</sub>. (iii) The number of mobile side-chains increases sharply at T<sub>d</sub> 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. This journal is</p>}}, author = {{Grimaldo, Marco and Roosen-Runge, Felix and Hennig, Marcus and Zanini, Fabio and Zhang, Fajun and Jalarvo, Niina and Zamponi, Michaela and Schreiber, Frank and Seydel, Tilo}}, issn = {{1463-9076}}, language = {{eng}}, month = {{02}}, number = {{6}}, pages = {{4645--4655}}, publisher = {{Royal Society of Chemistry}}, series = {{Physical Chemistry Chemical Physics}}, title = {{Hierarchical molecular dynamics of bovine serum albumin in concentrated aqueous solution below and above thermal denaturation}}, url = {{http://dx.doi.org/10.1039/c4cp04944f}}, doi = {{10.1039/c4cp04944f}}, volume = {{17}}, year = {{2015}}, }