Research output: Contribution to journal › Article › peer-review
High temperature and pressure influence the interdomain orientation of Nip7 proteins from P. abyssi and P. furiosus : MD simulations. / Medvedev, Kirill E.; Kolchanov, Nikolay A.; Afonnikov, Dmitry A.
In: Journal of Biomolecular Structure and Dynamics, Vol. 36, No. 1, 02.01.2018, p. 68-82.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - High temperature and pressure influence the interdomain orientation of Nip7 proteins from P. abyssi and P. furiosus
T2 - MD simulations
AU - Medvedev, Kirill E.
AU - Kolchanov, Nikolay A.
AU - Afonnikov, Dmitry A.
N1 - Publisher Copyright: © 2017 Informa UK Limited, trading as Taylor & Francis Group.
PY - 2018/1/2
Y1 - 2018/1/2
N2 - Interactions between protein domains and their position and movement relative to each other are essential for the stability and normal functioning of a protein molecule. Features of the movement of domains may define the mechanism of enzymatic reactions. Therefore, the description of this motion is an important task in the analysis of the structures and functions of multidomain proteins. In the current work, we investigated the influence of pressure and temperature on changes in the movement of the two domains of the protein Nip7, expressed by deep-water (Pyrococcus abyssi) and shallow-water (Pyrococcus furiosus) archaea. The results of the present study show that the interdomain interfaces of the Nip7 proteins of P. abyssi and P. furiosus are formed by stable hydrophobic interactions. It was shown that high pressure and high temperature significantly changed the orientation of domains in Nip7 proteins which perhaps was connected with functional features of these domains. It was found that increasing the pressure significantly changed the angle of rotation of these domains, to a greater extent in the shallow-water protein, while an increase in temperature slightly reduced the angle of rotation of these domains. Moreover, the results suggest that the type of motion of the domains under study is similar to shear motion.
AB - Interactions between protein domains and their position and movement relative to each other are essential for the stability and normal functioning of a protein molecule. Features of the movement of domains may define the mechanism of enzymatic reactions. Therefore, the description of this motion is an important task in the analysis of the structures and functions of multidomain proteins. In the current work, we investigated the influence of pressure and temperature on changes in the movement of the two domains of the protein Nip7, expressed by deep-water (Pyrococcus abyssi) and shallow-water (Pyrococcus furiosus) archaea. The results of the present study show that the interdomain interfaces of the Nip7 proteins of P. abyssi and P. furiosus are formed by stable hydrophobic interactions. It was shown that high pressure and high temperature significantly changed the orientation of domains in Nip7 proteins which perhaps was connected with functional features of these domains. It was found that increasing the pressure significantly changed the angle of rotation of these domains, to a greater extent in the shallow-water protein, while an increase in temperature slightly reduced the angle of rotation of these domains. Moreover, the results suggest that the type of motion of the domains under study is similar to shear motion.
KW - adaptation
KW - domain motions
KW - high temperature
KW - interdomain interface
KW - Nip7 protein
UR - http://www.scopus.com/inward/record.url?scp=85008147408&partnerID=8YFLogxK
U2 - 10.1080/07391102.2016.1268070
DO - 10.1080/07391102.2016.1268070
M3 - Article
C2 - 27924686
AN - SCOPUS:85008147408
VL - 36
SP - 68
EP - 82
JO - Journal of Biomolecular Structure and Dynamics
JF - Journal of Biomolecular Structure and Dynamics
SN - 0739-1102
IS - 1
ER -
ID: 10316154