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

• DOI: 10.1039/c4cp04944f
• Publication Date: 2015-01-07T11:03:56Z
• Authors: Marco Grimaldo; Felix Roosen-Runge; Marcus Hennig; Fabio Zanini; Fajun Zhang; Niina Jalarvo; Michaela Zamponi; Frank Schreiber; Tilo Seydel
• Keywords: Denaturation (fissile materials); Protein Dynamics; Dynamics; Bovine serum albumin; Nanosecond

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