Effects of High Hydrostatic Pressure on Proteins
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摘要: 在现有的超高压对蛋白质影响研究的基础上，详细地总结了超高压对蛋白质的分子体积、非共价键和分子结构的影响。在超高压作用下，蛋白质的分子体积被压缩变小；压力通过改变蛋白质分子的氢键、离子键、水合作用和疏水相互作用来影响蛋白质结构；低于800 MPa的压力会造成蛋白质分子的二级、三级和四级结构的改变，其中四级结构对压力最敏感，三级结构次之，二级结构的改变较小；高于8 GPa的压力会影响蛋白质分子的一级结构。Abstract: This review introduces the effects of high hydrostatic pressure on the molecular volume, non-covalent bond and conformation of protein.The molecular volume is decreased, and the hydrogen bond, electrovalent bond, and hydrophobic interaction are influenced by compression.The secondary, tertiary and quaternary structures of protein are influenced by pressure below 800 MPa.Tertiary and quaternary structures are more pressure-sensitive than secondary structure.Pressure below 8 GPa does not influence the primary structure of proteins.
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Key words:
- ultra-high pressure /
- protein /
- molecular volume /
- non-covalent bond /
- conformation
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表 1 超高压对蛋白质分子体积的影响
Table 1. Influences of ultra-high pressure on the molecular volume of proteins
Protein Pressure/(MPa) Molecular volume changes Test method Apomyoglobin 250 -61 mL/mol[15] Fluorescence Staphylococcal nuclease 100 -50 mL/mol[16] DSC Staphylococcal nuclease 300 -69--104 mL/mol[17] NMR, Fluorescence Bovine pancreatic ribonuclease 250 -21 mL/mol[14] NMR Flavodoxin from Peptostreptococcus elsdenii 870 -74 mL/mol[18] Fluorescence Flavodoxin from Desulfovibrio vulgaris 470 -63 mL/mol[18] Fluorescence Flavodoxin from Azotobacter vinelandii 1 060 -64 mL/mol[18] Fluorescence Metmyoglobin 60-600 -51--114 mL/mol[19] DSC, UV spectrum Cytochrome oxidase 250 -80 mL/mol[20] DSC, Visible spectrum Cytochrome b562 110 -102 mL/mol[21] NMR T4 lysozyme 200 -0.194 nm3[22] NMR, High pressure crystallography T4 lysozyme 50 -0.210 nm3[22] NMR, High pressure crystallography Note:DSC means differential scanning calorimetry; NMR means nuclear magnetic resonance. 
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表 2 超高压对蛋白质二级结构的影响
Table 2. Influences of ultra-high pressure on the secondary structure of proteins
Protein Pressure/(MPa) Changes of secondary structure Test method β-lactoglobulin 140 No change[43] FTIR β-lactoglobulin 600 The contents of α-helix and β-sheet decrease from
41% and 34% to 34% and 30%, respectively; The
content of random coil increases from 6% to 30%[44]Fourier transform Raman Ovalbumin 600 The content of α-helix decreases from 15% to 10%;
The contents of β-sheet and β-corner increase from
54% and 12% to 37% and 25%, respectively[44]Fourier transform Raman Ankyrin 100-600 35% of the α-helix structure is lost at 400 MPa[45] FTIR, SAXS Lysozyme 20-900 The secondary structure begins to change at
700 MPa; 54% of α-helix structure is lost
and all β-sheet disappear at 800 MPa[33]Raman Bovine pancreatic ribonuclease 0.1-1 400 The secondary structure is slightly changed at
570 MPa, and completely changed at 1 240 MPa[46]FTIR Note:FTIR means Fourier transform infrared spectroscopy.
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表 3 超高压对蛋白质三级结构的影响
Table 3. Influences of ultra-high pressure on the tertiary structure of proteins
Protein Pressure/(MPa) Changes of tertiary structure Test method Ubiquitin 600 The α-C-α-C distance between Leu 8 and Glu34 increases
from 0.9 nm to 1.5 nm, and the number of water
molecules per protein increases from 17.9 to 23.4[31]NMR Cytochrome P450 400 I-helix in the active site is changed[49-50] UV spectrum, Fluorescence Pancreatic trypsin inhibitor 200 The entire secondary and tertiary structures
are altered in the folded ensemble of
pancreatic trypsin inhibitor[51]NMR T4 lysozyme 200 The protein molecule exhibits a more compact
structure than the native; C-helix is removed
about 0.025 nm to the central[22]NMR, High pressure
crystallographyUrate oxidase 150 Volume of molecule is decreased by 0.3%;The polar
active-site increases by 11%, and the hydrophobic
cavity (0.19 nm3) decreases by 16%[37]Fluorescence, High pressure
crystallography
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表 4 超高压对蛋白质四级结构的影响
Table 4. Influences of ultra-high pressure on the quaternary structure of proteins
Protein Pressure/(MPa) Changes of quaternary structure Test method Urate oxidase (Four
monomers)150-175 The molecule is dissociated reversibly
at 150 MPa and irreversibly at
175 MPa followed by aggregation[37]Fluorescence,
High pressure
crystallographyLactate dehydrogenases
(Four monomers)100-200 The molecule is dissociated into
monomers at 200 MPa[53]Fluorescence β dimer tryptophan synthase 80-240 50% of the molecules are dissociated
at 220 MPa, and the conformation is
recovered in 2-3 min after compression[54]Fluorescence Yeast jexokinase (Dimer) 0.1-240 The molecules are completely
dissociated at 200 MPa[55]Fluorescence GorEL (Tetradecameric) and
GorES (Heptameric) from
Escherichia coli50-300 GorES and GorEL dissociate at 250 MPa;
GorES reassociate readily after high
pressure release, but GorEL does not[56]Electrophoresis,
UV spectrumEnolase (A tripolymer with
three subunits α, β, γ)0.1-300 Molecules are dissociated into
two parts at 300 MPa[57]Fluorescence Lactose repressor protein
(Tetramer)0.1-300 Molecules begin to dissociate at 160 MPa
and completely collapse at 280 MPa[58]Fluorescence, Visible
spectrumTriosephosphate isomerase 0.1-350 50% of the proteins dissociate at 260 MPa
and completely collapse at 350 MPa[59]Fluorescence, Size-
exclusion FPLCYeast glyceraldehyde phosphate
dehydrogenase (Tetramer)0.1-280 Molecules begin to dissociate at 120 MPa
and completely collapse at 200 MPa[60]Fluorescence Arc repressor (Dimer) 0-500 Arc repressor begins to dissociate at 100-200 MPa
and completely collapses at 300-500 MPa[52, 61]Two-dimensional NMR Note:FPLC means fast protein liquid chromatography.
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