The Experts below are selected from a list of 442842 Experts worldwide ranked by ideXlab platform
Robert S. Hodges - One of the best experts on this subject based on the ideXlab platform.
-
Intrinsic Amino Acid Side-Chain Hydrophilicity/Hydrophobicity Coefficients Determined by Reversed-Phase High-Performance Liquid Chromatography of Model Peptides: Comparison with Other Hydrophilicity/Hydrophobicity Scales
Biopolymers, 2009Co-Authors: Colin T. Mant, James M. Kovacs, Hyunmin Kim, David D. Pollock, Robert S. HodgesAbstract:An accurate determination of the intrinsic Hydrophilicity/hydrophobicity of amino acid side-chains in peptides and proteins is fundamental in understanding many area of research, including protein folding and stability, peptide and protein function, protein-protein interactions and peptide/protein oligomerization, as well as the design of protocols for purification and characterization of peptides and proteins. Our definition of intrinsic Hydrophilicity/hydrophobicity of side-chains is the maximum possible Hydrophilicity/hydrophobicity of side-chains in the absence of any nearest-neighbor effects and/or any conformational effects of the polypeptide chain that prevent full expression of side-chain Hydrophilicity/hydrophobicity. In this review, we have compared an experimentally derived intrinsic side-chain Hydrophilicity/hydrophobicity scale generated from RP-HPLC retention behavior of de novo designed synthetic model peptides at pH 2 and pH 7 with other RP-HPLC-derived scales, as well as scales generated from classic experimental and calculation-based methods of octanol/water partitioning of Nalpha-acetyl-amino-acid amides or free energy of transfer of free amino acids. Generally poor correlation was found with previous RP-HPLC-derived scales, likely due to the random nature of the peptide mixtures in terms of varying peptide size, conformation and frequency of particular amino acids. In addition, generally poor correlation with the classical approaches served to underline the importance of the presence of a polypeptide backbone when generating intrinsic values. We have shown that the intrinsic scale determined here is in full agreement with the structural characteristics of amino acid side-chains.
-
intrinsic amino acid side chain Hydrophilicity hydrophobicity coefficients determined by reversed phase high performance liquid chromatography of model peptides comparison with other Hydrophilicity hydrophobicity scales
Biopolymers, 2009Co-Authors: Colin T. Mant, James M. Kovacs, Hyunmin Kim, David D. Pollock, Robert S. HodgesAbstract:An accurate determination of the intrinsic Hydrophilicity/hydrophobicity of amino acid side-chains in peptides and proteins is fundamental in understanding many area of research, including protein folding and stability, peptide and protein function, protein-protein interactions and peptide/protein oligomerization, as well as the design of protocols for purification and characterization of peptides and proteins. Our definition of intrinsic Hydrophilicity/hydrophobicity of side-chains is the maximum possible Hydrophilicity/hydrophobicity of side-chains in the absence of any nearest-neighbor effects and/or any conformational effects of the polypeptide chain that prevent full expression of side-chain Hydrophilicity/hydrophobicity. In this review, we have compared an experimentally derived intrinsic side-chain Hydrophilicity/hydrophobicity scale generated from RP-HPLC retention behavior of de novo designed synthetic model peptides at pH 2 and pH 7 with other RP-HPLC-derived scales, as well as scales generated from classic experimental and calculation-based methods of octanol/water partitioning of Nalpha-acetyl-amino-acid amides or free energy of transfer of free amino acids. Generally poor correlation was found with previous RP-HPLC-derived scales, likely due to the random nature of the peptide mixtures in terms of varying peptide size, conformation and frequency of particular amino acids. In addition, generally poor correlation with the classical approaches served to underline the importance of the presence of a polypeptide backbone when generating intrinsic values. We have shown that the intrinsic scale determined here is in full agreement with the structural characteristics of amino acid side-chains.
Qiqing Zhang - One of the best experts on this subject based on the ideXlab platform.
-
amphiphilic poly vinyl chloride g poly poly ethylene glycol methylether methacrylate copolymer for the surface Hydrophilicity modification of poly vinylidene fluoride membrane
Journal of Applied Polymer Science, 2013Co-Authors: Xisheng Shao, Qing Zhou, Qiqing Zhang, Jianhua Li, Jing MiaoAbstract:In this study, a comblike amphiphilic graft copolymer containing poly(vinyl chloride) (PVC) backbones and poly(oxyethylene methacrylate) [poly(ethylene glycol) methylether methacrylate (PEGMA)] side chains was facilely synthesized via an atom transfer radical polymerization method. Secondary chlorines in PVC were used as initial sites to graft a poly[poly(ethylene glycol) methylether methacrylate] [P(PEGMA)] brush. The synthesized PVC-g-P(PEGMA) graft copolymer served as an efficient additive for the Hydrophilicity modification of the poly(vinylidene fluoride) (PVDF) membrane via a nonsolvent-induced phase-inversion technique. A larger pore size, higher porosity, and better connectivity were obtained for the modified PVDF membrane; this facilitated the permeability compared to the corresponding virgin PVDF membrane. In addition, the modified PVDF membrane showed a distinctively enhanced Hydrophilicity and antifouling resistance, as suggested by the contact angle measurement and flux of bovine serum albumin solution tests, respectively. Accordingly, the PVC-g-P(PEGMA) graft copolymer was demonstrated as a successful additive for the Hydrophilicity modification, and this study will likely open up new possibilities for the development of efficient amphiphilic PVC-based copolymers for the excellent Hydrophilicity modification of PVDF membranes. © 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci., 2013
-
the double effects of silver nanoparticles on the pvdf membrane surface Hydrophilicity and antifouling performance
Applied Surface Science, 2013Co-Authors: Xisheng Shao, Qing Zhou, Qiqing ZhangAbstract:Abstract In this study, silver nanoparticles were used to endow poly(vinylidene fluoride) (PVDF) membrane with excellent surface Hydrophilicity and outstanding antifouling performance. Silver nanoparticles were successfully immobilized onto PVDF membrane surface under the presence of poly(acrylic acid) (PAA). The double effects of silver nanoparticles on PVDF membrane, i.e., surface Hydrophilicity and anti-fouling performance, were systematically investigated. Judging from result of water static contact measurement, silver nanoparticles had provided a significant improvement in PVDF membrane surface Hydrophilicity. And the possible explanation on the improvement of PVDF membrane surface Hydrophilicity with silver nanoparticles was firstly proposed in this study. Membrane permeation and anti-bacterial tests were carried out to characterize the antifouling performance of PVDF membrane. Flux recovery ratio (FRR) increased about 40% after the presence of silver nanoparticles on the PVDF membrane surface, elucidating the anti-organic fouling performance of PVDF membrane was elevated by silver nanoparticles. Simultaneously, anti-bacterial test confirmed that PVDF membrane showed superior anti-biofouling activity because of silver nanoparticles. The above-mentioned results clarified that silver nanoparticles can endow PVDF membrane with both excellent surface Hydrophilicity and outstanding antifouling performance in this study.
Kazuhito Hashimoto - One of the best experts on this subject based on the ideXlab platform.
-
visible light induced Hydrophilicity on nitrogen substituted titanium dioxide films
Chemical Communications, 2003Co-Authors: Hiroshi Irie, Seitaro A Washizuka, Norio A Yoshino, Kazuhito HashimotoAbstract:Nitrogen-substituted titanium dioxide thin films were found to undergo hydrophilic conversion under irradiation with visible light. The Hydrophilicity was enhanced by increasing the degree of nitrogen substitution at oxygen sites. The water contact angle for the thin film with the greatest Hydrophilicity, TiO1.9884N0.0116, changed from 20 degrees to 6 degrees following irradiation.
-
visible light induced Hydrophilicity on nitrogen substituted titanium dioxide films
Chemical Communications, 2003Co-Authors: Hiroshi Irie, Seitaro A Washizuka, Norio A Yoshino, Kazuhito HashimotoAbstract:Nitrogen-substituted titanium dioxide thin films were found to undergo hydrophilic conversion under irradiation with visible light. The Hydrophilicity was enhanced by increasing the degree of nitrogen substitution at oxygen sites. The water contact angle for the thin film with the greatest Hydrophilicity, TiO1.9884N0.0116, changed from 20° to 6° following irradiation.
-
photocatalysis and photoinduced Hydrophilicity of various metal oxide thin films
Chemistry of Materials, 2002Co-Authors: Masahiro Miyauchi, Akira Nakajima, Toshiya Watanabe And, Kazuhito HashimotoAbstract:Thin films of various metal oxides were prepared on glass substrates by a wet process to determine their photocatalytic ability to decompose adsorbed dye and to evaluate their photoinduced Hydrophilicity under UV illumination. The metal oxides used in this study are classified into four categories based on their behavior over the two photochemical reaction: (1) active in both photocatalytic oxidation and photoinduced Hydrophilicity (TiO2, SnO2, ZnO); (2) only active in photocatalytic oxidation (SrTiO3); (3) only active in photoinduced Hydrophilicity (WO3, V2O5); (4) and inactive over both processes (CeO2, CuO, MoO3, Fe2O3, Cr2O3, In2O3). X-ray photoelectron spectroscopy revealed that oxygen defect sites were produced by Ar+ bombardment on the surface of metal oxides, showing photoinduced Hydrophilicity. These results indicate that photoinduced Hydrophilicity is not induced by the photocatalytic oxidation of organic compounds adsorbed on the surface, but is based on structural changes of the metal oxide s...
Colin T. Mant - One of the best experts on this subject based on the ideXlab platform.
-
Intrinsic Amino Acid Side-Chain Hydrophilicity/Hydrophobicity Coefficients Determined by Reversed-Phase High-Performance Liquid Chromatography of Model Peptides: Comparison with Other Hydrophilicity/Hydrophobicity Scales
Biopolymers, 2009Co-Authors: Colin T. Mant, James M. Kovacs, Hyunmin Kim, David D. Pollock, Robert S. HodgesAbstract:An accurate determination of the intrinsic Hydrophilicity/hydrophobicity of amino acid side-chains in peptides and proteins is fundamental in understanding many area of research, including protein folding and stability, peptide and protein function, protein-protein interactions and peptide/protein oligomerization, as well as the design of protocols for purification and characterization of peptides and proteins. Our definition of intrinsic Hydrophilicity/hydrophobicity of side-chains is the maximum possible Hydrophilicity/hydrophobicity of side-chains in the absence of any nearest-neighbor effects and/or any conformational effects of the polypeptide chain that prevent full expression of side-chain Hydrophilicity/hydrophobicity. In this review, we have compared an experimentally derived intrinsic side-chain Hydrophilicity/hydrophobicity scale generated from RP-HPLC retention behavior of de novo designed synthetic model peptides at pH 2 and pH 7 with other RP-HPLC-derived scales, as well as scales generated from classic experimental and calculation-based methods of octanol/water partitioning of Nalpha-acetyl-amino-acid amides or free energy of transfer of free amino acids. Generally poor correlation was found with previous RP-HPLC-derived scales, likely due to the random nature of the peptide mixtures in terms of varying peptide size, conformation and frequency of particular amino acids. In addition, generally poor correlation with the classical approaches served to underline the importance of the presence of a polypeptide backbone when generating intrinsic values. We have shown that the intrinsic scale determined here is in full agreement with the structural characteristics of amino acid side-chains.
-
intrinsic amino acid side chain Hydrophilicity hydrophobicity coefficients determined by reversed phase high performance liquid chromatography of model peptides comparison with other Hydrophilicity hydrophobicity scales
Biopolymers, 2009Co-Authors: Colin T. Mant, James M. Kovacs, Hyunmin Kim, David D. Pollock, Robert S. HodgesAbstract:An accurate determination of the intrinsic Hydrophilicity/hydrophobicity of amino acid side-chains in peptides and proteins is fundamental in understanding many area of research, including protein folding and stability, peptide and protein function, protein-protein interactions and peptide/protein oligomerization, as well as the design of protocols for purification and characterization of peptides and proteins. Our definition of intrinsic Hydrophilicity/hydrophobicity of side-chains is the maximum possible Hydrophilicity/hydrophobicity of side-chains in the absence of any nearest-neighbor effects and/or any conformational effects of the polypeptide chain that prevent full expression of side-chain Hydrophilicity/hydrophobicity. In this review, we have compared an experimentally derived intrinsic side-chain Hydrophilicity/hydrophobicity scale generated from RP-HPLC retention behavior of de novo designed synthetic model peptides at pH 2 and pH 7 with other RP-HPLC-derived scales, as well as scales generated from classic experimental and calculation-based methods of octanol/water partitioning of Nalpha-acetyl-amino-acid amides or free energy of transfer of free amino acids. Generally poor correlation was found with previous RP-HPLC-derived scales, likely due to the random nature of the peptide mixtures in terms of varying peptide size, conformation and frequency of particular amino acids. In addition, generally poor correlation with the classical approaches served to underline the importance of the presence of a polypeptide backbone when generating intrinsic values. We have shown that the intrinsic scale determined here is in full agreement with the structural characteristics of amino acid side-chains.
David D. Pollock - One of the best experts on this subject based on the ideXlab platform.
-
Intrinsic Amino Acid Side-Chain Hydrophilicity/Hydrophobicity Coefficients Determined by Reversed-Phase High-Performance Liquid Chromatography of Model Peptides: Comparison with Other Hydrophilicity/Hydrophobicity Scales
Biopolymers, 2009Co-Authors: Colin T. Mant, James M. Kovacs, Hyunmin Kim, David D. Pollock, Robert S. HodgesAbstract:An accurate determination of the intrinsic Hydrophilicity/hydrophobicity of amino acid side-chains in peptides and proteins is fundamental in understanding many area of research, including protein folding and stability, peptide and protein function, protein-protein interactions and peptide/protein oligomerization, as well as the design of protocols for purification and characterization of peptides and proteins. Our definition of intrinsic Hydrophilicity/hydrophobicity of side-chains is the maximum possible Hydrophilicity/hydrophobicity of side-chains in the absence of any nearest-neighbor effects and/or any conformational effects of the polypeptide chain that prevent full expression of side-chain Hydrophilicity/hydrophobicity. In this review, we have compared an experimentally derived intrinsic side-chain Hydrophilicity/hydrophobicity scale generated from RP-HPLC retention behavior of de novo designed synthetic model peptides at pH 2 and pH 7 with other RP-HPLC-derived scales, as well as scales generated from classic experimental and calculation-based methods of octanol/water partitioning of Nalpha-acetyl-amino-acid amides or free energy of transfer of free amino acids. Generally poor correlation was found with previous RP-HPLC-derived scales, likely due to the random nature of the peptide mixtures in terms of varying peptide size, conformation and frequency of particular amino acids. In addition, generally poor correlation with the classical approaches served to underline the importance of the presence of a polypeptide backbone when generating intrinsic values. We have shown that the intrinsic scale determined here is in full agreement with the structural characteristics of amino acid side-chains.
-
intrinsic amino acid side chain Hydrophilicity hydrophobicity coefficients determined by reversed phase high performance liquid chromatography of model peptides comparison with other Hydrophilicity hydrophobicity scales
Biopolymers, 2009Co-Authors: Colin T. Mant, James M. Kovacs, Hyunmin Kim, David D. Pollock, Robert S. HodgesAbstract:An accurate determination of the intrinsic Hydrophilicity/hydrophobicity of amino acid side-chains in peptides and proteins is fundamental in understanding many area of research, including protein folding and stability, peptide and protein function, protein-protein interactions and peptide/protein oligomerization, as well as the design of protocols for purification and characterization of peptides and proteins. Our definition of intrinsic Hydrophilicity/hydrophobicity of side-chains is the maximum possible Hydrophilicity/hydrophobicity of side-chains in the absence of any nearest-neighbor effects and/or any conformational effects of the polypeptide chain that prevent full expression of side-chain Hydrophilicity/hydrophobicity. In this review, we have compared an experimentally derived intrinsic side-chain Hydrophilicity/hydrophobicity scale generated from RP-HPLC retention behavior of de novo designed synthetic model peptides at pH 2 and pH 7 with other RP-HPLC-derived scales, as well as scales generated from classic experimental and calculation-based methods of octanol/water partitioning of Nalpha-acetyl-amino-acid amides or free energy of transfer of free amino acids. Generally poor correlation was found with previous RP-HPLC-derived scales, likely due to the random nature of the peptide mixtures in terms of varying peptide size, conformation and frequency of particular amino acids. In addition, generally poor correlation with the classical approaches served to underline the importance of the presence of a polypeptide backbone when generating intrinsic values. We have shown that the intrinsic scale determined here is in full agreement with the structural characteristics of amino acid side-chains.
