Hydrophobic Side Chain Interactions in Synthetic Polypeptides and Proteins at the Air-Water Interface

1975 ◽  
pp. 338-359 ◽  
Author(s):  
B. R. MALCOLM
Keyword(s):  
Side Chain ◽  
Water Interface ◽  
Synthetic Polypeptides ◽  
Air Water Interface

scholarly journals Effect of Urea on Hydrophobic Side Chain Interactions in Polypeptides at the Air–Water Interface

1984 ◽  
Vol 57 (3) ◽  
pp. 873-874 ◽  
Author(s):  
Akira Shibata ◽  
Shinsuke Yamashita ◽  
Takuya Yamashita
Keyword(s):  
Side Chain ◽  
Water Interface ◽  
Air Water Interface

scholarly journals Methylguanidinium at the Air/Water Interface: A Simulation Study with the Drude Polarizable Force Field

2020 ◽  
Author(s):  
Jian Zhu ◽  
Jing Huang
Keyword(s):  
Force Field ◽  
Model Compound ◽  
Side Chain ◽  
Water Interface ◽  
Polarizable Force Field ◽  
Polarization Effects ◽  
Structure And Dynamics ◽  
Arginine Side Chain ◽  
Air Water Interface ◽  
Dynamics Simulations

<div>Methylguanidinium is an important molecular ion which also serves as the model compound for arginine side chain. We studied the structure and dynamics of methylguanidium ion at the air/water interface by molecular dynamics simulations employing the Drude polarizable force field. We found out that methylguanidinium accumulate on the interface with a majority adopting tilted conformations. We also demonstrated that methylguanidinium and guanidinium ions have different preference towards the air/water interface. Our results illustrate the importance to explicitly include the electronic polarization effects in modeling interfacial properties.</div><div><br> </div>

The interaction between synthetic polypeptides and fatty acids at the air/water interface

1988 ◽  
Vol 124 (1) ◽  
pp. 290-300 ◽  
Author(s):  
Fumiko Kimura ◽  
Shogo Uematsu ◽  
Hisako Sakurai ◽  
Yukio Akahori ◽  
Masayuki Nakagaki
Keyword(s):  
Fatty Acids ◽  
Water Interface ◽  
Synthetic Polypeptides ◽  
Air Water Interface

scholarly journals Ubiquinones have surface-active properties suited to transport electrons and protons across membranes

1980 ◽  
Vol 185 (3) ◽  
pp. 715-722 ◽  
Author(s):  
Peter J. Quinn ◽  
Manouchehre A. Esfahani
Keyword(s):  
Fatty Acyl ◽  
Side Chain ◽  
Water Interface ◽  
Collapse Pressure ◽  
Phospholipid Monolayer ◽  
Ideal Mixing ◽  
Surface Active Properties ◽  
Air Water Interface ◽  
Surface Active ◽  
Ubiquinone 10

Surface-active properties of ubiquinones and ubiquinols have been investigated by monomolecular-film techniques. Stable monolayers are formed at an air/water interface by the fully oxidized and reduced forms of the coenzyme; collapse pressures and hence stability of the films tend to increase with decreasing length of the isoprenoid side chain and films of the reduced coenzymes are more stable than those of their oxidized counterparts. Ubiquinone with a side chain of two isoprenoid units does not form stable monolayers at the air/water interface. Mixed monolayers of ubiquinol-10 or ubiquinone-10 with 1,2-dimyristoyl phosphatidylcholine, soya phosphatidylcholine and diphosphatidylglycerol do not exhibit ideal mixing characteristics. At surface pressures less than the collapse pressure of pure ubiquinone-10 monolayers (approx. 12mN·m−1) the isoprenoid chain is located substantially within the region occupied by the fatty acyl residues of the phospholipids. With increasing surface pressure the ubiquinones and their fully reduced equivalents are progressively squeezed out from between the phospholipid molecules until, at a pressure of about 35mN·m−1, the film has surface properties consistent with that of the pure phospholipid monolayer. This suggests that the ubiquinone(ol) forms a separate phase overlying the phospholipid monolayer. The implications of this energetically poised situation, where the quinone(ol) is just able to penetrate the phospholipid film, are considered in terms of the function of ubiquinone(ol) as electron and proton carriers of energy-transducing membranes.

Side chain assisted nanotubular self-assembly of cyclic peptides at the air–water interface

Soft Matter ◽  
2010 ◽  
Vol 6 (19) ◽  
pp. 4701 ◽  
Author(s):  
Byeongdo Kwak ◽  
Kwanwoo Shin ◽  
Sangjun Seok ◽  
Doseok Kim ◽  
Farhan Ahmad ◽  
...  
Keyword(s):  
Self Assembly ◽  
Cyclic Peptides ◽  
Side Chain ◽  
Water Interface ◽  
Air Water Interface

scholarly journals Slow structural rearrangement of a side-chain phthalocyanine methacrylate polymer at the air-water interface

1993 ◽  
Vol 26 (13) ◽  
pp. 3306-3312 ◽  
Author(s):  
C. F. van Nostrum ◽  
R. J. M. Nolte ◽  
M. A. C. Devillers ◽  
G. T. Oostergetel ◽  
M. N. Teerenstra ◽  
...  
Keyword(s):  
Structural Rearrangement ◽  
Side Chain ◽  
Water Interface ◽  
Air Water Interface

scholarly journals Methylguanidinium at the Air/Water Interface: A Simulation Study with the Drude Polarizable Force Field

2020 ◽  
Author(s):  
Jian Zhu ◽  
Jing Huang
Keyword(s):  
Force Field ◽  
Model Compound ◽  
Side Chain ◽  
Water Interface ◽  
Polarizable Force Field ◽  
Polarization Effects ◽  
Structure And Dynamics ◽  
Arginine Side Chain ◽  
Air Water Interface ◽  
Dynamics Simulations

<div>Methylguanidinium is an important molecular ion which also serves as the model compound for arginine side chain. We studied the structure and dynamics of methylguanidium ion at the air/water interface by molecular dynamics simulations employing the Drude polarizable force field. We found out that methylguanidinium accumulate on the interface with a majority adopting tilted conformations. We also demonstrated that methylguanidinium and guanidinium ions have different preference towards the air/water interface. Our results illustrate the importance to explicitly include the electronic polarization effects in modeling interfacial properties.</div><div><br> </div>

scholarly journals Methylguanidinium at the Air/Water Interface: A Simulation Study with the Drude Polarizable Force Field

2020 ◽  
Author(s):  
Jian Zhu ◽  
Jing Huang
Keyword(s):  
Force Field ◽  
Model Compound ◽  
Side Chain ◽  
Water Interface ◽  
Polarizable Force Field ◽  
Polarization Effects ◽  
Structure And Dynamics ◽  
Arginine Side Chain ◽  
Air Water Interface ◽  
Dynamics Simulations

<div>Methylguanidinium is an important molecular ion which also serves as the model compound for arginine side chain. We studied the structure and dynamics of methylguanidium ion at the air/water interface by molecular dynamics simulations employing the Drude polarizable force field. We found out that methylguanidinium accumulate on the interface with a majority adopting tilted conformations. We also demonstrated that methylguanidinium and guanidinium ions have different preference towards the air/water interface. Our results illustrate the importance to explicitly include the electronic polarization effects in modeling interfacial properties.</div><div><br> </div>

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