title: Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
metadata.name: dc.contributor.author
metadata.value: Kurauskas, Vilius
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Izmailov, Sergei A
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Rogacheva, Olga N
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Hessel, Audrey
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Ayala, Isabel
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Woodhouse, Joyce
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Shilova, Anastasya
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Xue, Yi
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Yuwen, Tairan
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Coquelle, Nicolas
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Colletier, Jacques-Philippe
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Skrynnikov, Nikolai R
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Schanda, Paul
metadata.lang: -
metadata.name: dc.date.accessioned
metadata.value: 2017-08-08T12:38:13Z
metadata.lang: -
metadata.name: dc.date.available
metadata.value: 2017-08-08T12:38:13Z
metadata.lang: -
metadata.name: dc.date.issued
metadata.value: 2017-07-27
metadata.lang: -
metadata.name: dc.identifier
metadata.value: 10.1038/s41467-017-00165-8
metadata.lang: -
metadata.name: dc.identifier.citation
metadata.value: Kurauskas, V.; Izmailov, S. A.; Rogacheva, O. N.; Hessel, A.; Ayala, I.; Woodhouse, J.; Shilova, A.; Xue, Y.; Yuwen, T.; Coquelle, N.; Colletier, J.-P.; Skrynnikov, N. R.; Schanda, P. Slow Conformational Exchange and Overall Rocking Motion in Ubiquitin Protein Crystals. Nature Communications 2017, 8 (1), 145 DOI: 10.1038/s41467-017-00165-8. https://www.nature.com/articles/s41467-017-00165-8
metadata.lang: en_GB
metadata.name: dc.identifier.other
metadata.value: 10.1038/s41467-017-00165-8
metadata.lang: -
metadata.name: dc.identifier.other
metadata.value: 10.1038/s41467-017-00165-8
metadata.lang: -
metadata.name: dc.identifier.uri
metadata.value: https://www.nature.com/articles/s41467-017-00165-8
metadata.lang: -
metadata.name: dc.identifier.uri
metadata.value: http://hdl.handle.net/11701/7027
metadata.lang: -
metadata.name: dc.description.abstract
metadata.value: Proteins perform their functions in solution but their structures are most frequently studied inside crystals. Here we probe how the crystal packing alters microsecond dynamics, using solid-state NMR measurements and multi-microsecond MD simulations of different crystal forms of ubiquitin. In particular, near-rotary-resonance relaxation dispersion (NERRD) experiments probe angular backbone motion, while Bloch-McConnell relaxation dispersion data report on fluctuations of the local electronic environment. These experiments and simulations reveal that the packing of the protein can significantly alter the thermodynamics and kinetics of local conformational exchange. Moreover, we report small-amplitude reorientational motion of protein molecules in the crystal lattice with an ~3-5° amplitude on a tens-of-microseconds time scale in one of the crystals, but not in others. An intriguing possibility arises that overall motion is to some extent coupled to local dynamics. Our study highlights the importance of considering the packing when analyzing dynamics of crystalline proteins.X-ray crystallography is the main method for protein structure determination. Here the authors combine solid-state NMR measurements and molecular dynamics simulations and show that crystal packing alters the thermodynamics and kinetics of local conformational exchange as well as overall rocking motion of protein molecules in the crystal lattice.
metadata.lang: en_GB
metadata.name: dc.language.iso
metadata.value: en
metadata.lang: en_GB
metadata.name: dc.publisher
metadata.value: Macmillan Publishers Limited, part of Springer Nature.
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: protein
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: crystal
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: dynamics
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: ubiquitin
metadata.lang: en_GB
metadata.name: dc.title
metadata.value: Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
metadata.lang: en_GB
metadata.name: dc.type
metadata.value: Article
metadata.lang: en_GB
resources.filename: s41467-017-00165-8.pdf
resources.url: https://dspace.spbu.ru/bitstream/11701/7027/1/s41467-017-00165-8.pdf
resources.format: Adobe PDF
resources.size: 1,68 MB