Rehydration Post-orientation: Investigating Field-Induced Structural Changes via Computational Rehydration

被引:5
作者
Brodmerkel, Maxim N. [1 ]
De Santis, Emiliano [1 ,2 ]
Caleman, Carl [2 ,3 ]
Marklund, Erik G. [1 ]
机构
[1] Uppsala Univ, Dept Chem BMC, Box 576, S-75123 Uppsala, Sweden
[2] Uppsala Univ, Dept Phys & Astron, S-75120 Uppsala, Sweden
[3] DESY, Ctr Free Electron Laser Sci, Notkestr 85, D-22607 Hamburg, Germany
基金
欧盟地平线“2020”; 瑞典研究理事会;
关键词
Molecular dynamics simulation; Protein hydration; Electric dipole; Protein structure; Structural biology; X-rays; MOBILITY-MASS-SPECTROMETRY; C-TERMINAL FRAGMENT; MOLECULAR-DYNAMICS SIMULATIONS; L7/L12; RIBOSOMAL-PROTEIN; COLLISION CROSS-SECTIONS; GAS-PHASE; TRP-CAGE; ELECTRON-MICROSCOPY; STABILITY; UBIQUITIN;
D O I
10.1007/s10930-023-10110-y
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Proteins can be oriented in the gas phase using strong electric fields, which brings advantages for structure determination using X-ray free electron lasers. Both the vacuum conditions and the electric-field exposure risk damaging the protein structures. Here, we employ molecular dynamics simulations to rehydrate and relax vacuum and electric-field exposed proteins in aqueous solution, which simulates a refinement of structure models derived from oriented gas-phase proteins. We find that the impact of the strong electric fields on the protein structures is of minor importance after rehydration, compared to that of vacuum exposure and ionization in electrospraying. The structures did not fully relax back to their native structure in solution on the simulated timescales of 200 ns, but they recover several features, including native-like intra-protein contacts, which suggests that the structures remain in a state from which the fully native structure is accessible. Our findings imply that the electric fields used in native mass spectrometry are well below a destructive level, and suggest that structures inferred from X-ray diffraction from gas-phase proteins are relevant for solution and in vivo conditions, at least after in silico rehydration.
引用
收藏
页码:205 / 218
页数:14
相关论文
共 74 条
  • [1] All-atom simulations of crowding effects on ubiquitin dynamics
    Abriata, Luciano A.
    Spiga, Enrico
    Dal Peraro, Matteo
    [J]. PHYSICAL BIOLOGY, 2013, 10 (04)
  • [2] Alonso DOV, 1998, PROTEIN SCI, V7, P860
  • [3] MOLECULAR-DYNAMICS SIMULATION OF THE SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT OF L7/L12 RIBOSOMAL-PROTEIN
    AQVIST, J
    TAPIA, O
    [J]. BIOPOLYMERS, 1990, 30 (1-2) : 205 - 209
  • [4] A MOLECULAR-DYNAMICS STUDY OF THE C-TERMINAL FRAGMENT OF THE L7/L12 RIBOSOMAL-PROTEIN - SECONDARY STRUCTURE MOTION IN A 150 PICOSECOND TRAJECTORY
    AQVIST, J
    VANGUNSTEREN, WF
    LEIJONMARCK, M
    TAPIA, O
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1985, 183 (03) : 461 - 477
  • [5] Protein Ions Generated by Native Electrospray Ionization: Comparison of Gas Phase, Solution, and Crystal Structures
    Bakhtiari, Maryam
    Konermann, Lars
    [J]. JOURNAL OF PHYSICAL CHEMISTRY B, 2019, 123 (08) : 1784 - 1796
  • [6] Determinants of miniprotein stability: can anything replace a buried H-bonded Trp sidechain?
    Barua, B
    Andersen, NH
    [J]. LETTERS IN PEPTIDE SCIENCE, 2001, 8 (3-5): : 221 - 226
  • [7] The Trp-cage: optimizing the stability of a globular miniprotein
    Barua, Bipasha
    Lin, Jasper C.
    Williams, Victoria D.
    Kummler, Phillip
    Neidigh, Jonathan W.
    Andersen, Niels H.
    [J]. PROTEIN ENGINEERING DESIGN & SELECTION, 2008, 21 (03) : 171 - 185
  • [8] Mass spectrometry: come of age for structural and dynamical biology
    Benesch, Justin L. P.
    Ruotolo, Brandon T.
    [J]. CURRENT OPINION IN STRUCTURAL BIOLOGY, 2011, 21 (05) : 641 - 649
  • [9] MOLECULAR-DYNAMICS WITH COUPLING TO AN EXTERNAL BATH
    BERENDSEN, HJC
    POSTMA, JPM
    VANGUNSTEREN, WF
    DINOLA, A
    HAAK, JR
    [J]. JOURNAL OF CHEMICAL PHYSICS, 1984, 81 (08) : 3684 - 3690
  • [10] STRUCTURE OF HEN EGG-WHITE LYSOZYME - A 3-DIMENSIONAL FOURIER SYNTHESIS AT 2A RESOLUTION
    BLAKE, CCF
    KOENIG, DF
    MAIR, GA
    NORTH, ACT
    PHILLIPS, DC
    SARMA, VR
    [J]. NATURE, 1965, 206 (4986) : 757 - &