NEW APPROACHES TO SLOW DYNAMICS OF PROTEIN DOMAINS

被引:0
|
作者
Yesylevskyy, S. O. [1 ]
Kharkyanen, V. N. [1 ]
机构
[1] Natl Acad Sci Ukraine, Inst Phys, 46 Nauky Prosp, UA-03039 Kiev, Ukraine
来源
UKRAINIAN JOURNAL OF PHYSICS | 2009年 / 54卷 / 1-2期
关键词
D O I
暂无
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
Proteins are very familiar objects for biologists and biophysicists. However, from the point of view of the physicist the proteins are mysterious objects, which cannot be compared with any other object in nature. What really set the proteins apart from any other physical system are their motions. The time scale of protein motions covers 15-16 orders of magnitude and extends from 10(-1)3 s to minutes or even hours. This is probably the broadest spectrum of motions observable in any other physical system of comparable size. The fastest motions are localized and mostly harmonic. In contrast, the slowest motions are collective (delocalized), strongly inharmonic and dissipative (diffusive). Functioning of the proteins in living cells require subtle balance between the motions with very different time scales. Large scale slow motions are critical for the functioning of numerous enzymes, transport proteins, molecular motors, ion channels and other proteins. In this work we provide systematic analysis of our recent developments in the field of slow protein dynamics based on the concepts of dynamic domains and fuzzy domains.
引用
收藏
页码:109 / 116
页数:8
相关论文
共 50 条
  • [1] Harmonicity in slow protein dynamics
    Hinsen, K
    Petrescu, AJ
    Dellerue, S
    Bellissent-Funel, MC
    Kneller, GR
    [J]. CHEMICAL PHYSICS, 2000, 261 (1-2) : 25 - 37
  • [2] Increased slow dynamics defines ligandability of BTB domains
    Vladlena Kharchenko
    Brian M. Linhares
    Megan Borregard
    Iwona Czaban
    Jolanta Grembecka
    Mariusz Jaremko
    Tomasz Cierpicki
    Łukasz Jaremko
    [J]. Nature Communications, 13
  • [3] Increased slow dynamics defines ligandability of BTB domains
    Kharchenko, Vladlena
    Linhares, Brian M.
    Borregard, Megan
    Czaban, Iwona
    Grembecka, Jolanta
    Jaremko, Mariusz
    Cierpicki, Tomasz
    Jaremko, Lukasz
    [J]. NATURE COMMUNICATIONS, 2022, 13 (01)
  • [4] New approaches to the mapping of chromosomal domains
    Filipski, J
    Svetlova, E
    AvrilFournout, N
    Deschavanne, P
    Bellis, M
    [J]. ACTA BIOCHIMICA POLONICA, 1996, 43 (02) : 289 - 292
  • [5] Slow internal protein dynamics in solution
    Biehl, R.
    Richter, D.
    [J]. JOURNAL OF PHYSICS-CONDENSED MATTER, 2014, 26 (50)
  • [6] Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions
    Rossi, Maria-Agustina
    Palzkill, Timothy
    Almeida, Fabio C. L.
    Vila, Alejandro J.
    [J]. MOLECULAR BIOLOGY AND EVOLUTION, 2022, 39 (10)
  • [7] New approaches to track chemoenzymatic loading reactions of NRPS carrier protein domains using NMR
    Marincin, Kenneth A.
    Hwang, Yousang
    Kengmana, Everett S.
    Meyers, David J.
    Frueh, Dominique P.
    [J]. BIOPHYSICAL JOURNAL, 2023, 122 (03) : 286A - 287A
  • [8] DYNAMICS OF FORMATION AND KINETICS OF MOTION OF SLOW DOMAINS IN GALLIUM-ARSENIDE
    SHISHIYANU, FS
    [J]. SOVIET PHYSICS SEMICONDUCTORS-USSR, 1975, 9 (01): : 11 - 14
  • [9] Nature of slow dynamics in a minimal model of frustration-limited domains
    Geissler, PL
    Reichman, DR
    [J]. PHYSICAL REVIEW E, 2004, 69 (02): : 021501 - 1
  • [10] Slow conformational dynamics in the hamster prion protein
    Kuwata, K
    Kamatari, YO
    Akasaka, K
    James, TL
    [J]. BIOCHEMISTRY, 2004, 43 (15) : 4439 - 4446