Quantitative and qualitative analysis of type III antifreeze protein structure and function
about
The Refined Crystal Structure of an Eel Pout Type III Antifreeze Protein RD1 at 0.62-Å Resolution Reveals Structural Microheterogeneity of Protein and SolvationNMR structure note: a defective isoform and its activity-improved variant of a type III antifreeze protein from Zoarces elongates KnerEngineering a naturally inactive isoform of type III antifreeze protein into one that can stop the growth of ice.Structure of type I antifreeze protein and mutants in supercooled water.Analysis of ice-binding sites in fish type II antifreeze protein by quantum mechanics.Identification of antifreeze proteins and their functional residues by support vector machine and genetic algorithms based on n-peptide compositions.Cell biology in the Antarctic: studying life in the freezer.Observation of ice-like water layers at an aqueous protein surface.Crystallization and preliminary X-ray crystallographic analysis of Ca2+-independent and Ca2+-dependent species of the type II antifreeze proteinPerdeuteration, purification, crystallization and preliminary neutron diffraction of an ocean pout type III antifreeze protein.Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential CryoprotectantIce-binding surface of fish type III antifreeze.Modeling Pseudomonas syringae ice-nucleation protein as a beta-helical protein.Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase.Thermodynamic stability of a cold-adapted protein, type III antifreeze protein, and energetic contribution of salt bridges.Co-operative effect of the isoforms of type III antifreeze protein expressed in Notched-fin eelpout, Zoarces elongatus Kner.Structure and collective dynamics of hydrated anti-freeze protein type III from 180 K to 298 K by X-ray diffraction and inelastic X-ray scattering.Fully active QAE isoform confers thermal hysteresis activity on a defective SP isoform of type III antifreeze protein.Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions.NMR study of the antifreeze activities of active and inactive isoforms of a type III antifreeze protein.Structure of solvation water around the active and inactive regions of a type III antifreeze protein and its mutants of lowered activity.
P2860
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P2860
Quantitative and qualitative analysis of type III antifreeze protein structure and function
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
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name
Quantitative and qualitative a ...... protein structure and function
@ast
Quantitative and qualitative a ...... protein structure and function
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Quantitative and qualitative a ...... protein structure and function
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type
label
Quantitative and qualitative a ...... protein structure and function
@ast
Quantitative and qualitative a ...... protein structure and function
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Quantitative and qualitative a ...... protein structure and function
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prefLabel
Quantitative and qualitative a ...... protein structure and function
@ast
Quantitative and qualitative a ...... protein structure and function
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Quantitative and qualitative a ...... protein structure and function
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P2093
P2860
P356
P1476
Quantitative and qualitative a ...... protein structure and function
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P2093
P2860
P304
P356
10.1074/JBC.274.17.11842
P407
P577
1999-04-23T00:00:00Z