Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. / Kurauskas, Vilius; Izmailov, Sergei A.; Rogacheva, Olga N.; Hessel, Audrey; Ayala, Isabel; Woodhouse, Joyce; Shilova, Anastasya; Xue, Yi; Yuwen, Tairan; Coquelle, Nicolas; Colletier, Jacques Philippe; Skrynnikov, Nikolai R.; Schanda, Paul.
в: Nature Communications, Том 8, № 1, 145, 01.12.2017.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
}
TY - JOUR
T1 - Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
AU - Kurauskas, Vilius
AU - Izmailov, Sergei A.
AU - Rogacheva, Olga N.
AU - Hessel, Audrey
AU - Ayala, Isabel
AU - Woodhouse, Joyce
AU - Shilova, Anastasya
AU - Xue, Yi
AU - Yuwen, Tairan
AU - Coquelle, Nicolas
AU - Colletier, Jacques Philippe
AU - Skrynnikov, Nikolai R.
AU - Schanda, Paul
N1 - Publisher Copyright: © 2017 The Author(s). Copyright: Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2017/12/1
Y1 - 2017/12/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85026325162&partnerID=8YFLogxK
U2 - 10.1038/s41467-017-00165-8
DO - 10.1038/s41467-017-00165-8
M3 - Article
C2 - 28747759
VL - 8
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
M1 - 145
ER -
ID: 7756974