Isolated Monohydrates of a Model Peptide Chain: Effect of a First Water Molecule on the Secondary Structure of a Capped Phenylalanine

2011 ◽  
Vol 133 (11) ◽  
pp. 3931-3942 ◽  
Author(s):  
Himansu S. Biswal ◽  
Yohan Loquais ◽  
Benjamin Tardivel ◽  
Eric Gloaguen ◽  
Michel Mons
Keyword(s):  
Secondary Structure ◽  
Water Molecule ◽  
Peptide Chain ◽  
Model Peptide

Far/Mid-Infrared Signatures of Solvent–Solute Interactions in a Microhydrated Model Peptide Chain

2012 ◽  
Vol 3 (22) ◽  
pp. 3307-3311 ◽  
Author(s):  
Manuela Cirtog ◽  
Anouk M. Rijs ◽  
Yohan Loquais ◽  
Valérie Brenner ◽  
Benjamin Tardivel ◽  
...  
Keyword(s):  
Peptide Chain ◽  
Model Peptide ◽  
Mid Infrared ◽  
Solute Interactions

Effects of truncation of the peptide chain on the secondary structure and bioactivities of palmitoylated anoplin

Peptides ◽  
2018 ◽  
Vol 104 ◽  
pp. 7-14 ◽  
Author(s):  
Remmer L. Salas ◽  
Jan Kathryne D.L. Garcia ◽  
Ana Carmela R. Miranda ◽  
Windell L. Rivera ◽  
Ricky B. Nellas ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Peptide Chain

scholarly journals A water molecule participates in the secondary structure of hyaluronan

1988 ◽  
Vol 254 (2) ◽  
pp. 489-493 ◽  
Author(s):  
F Heatley ◽  
J E Scott
Keyword(s):  
Secondary Structure ◽  
Water Molecule ◽  
High Field ◽  
Cell Membranes ◽  
Proton Exchange ◽  
Dimethyl Sulphoxide ◽  
Molecular Models ◽  
Saturation Transfer ◽  
Water Bridge ◽  
Space Filling

The structure of hyaluronan was investigated in water/dimethyl sulphoxide mixtures by using high-field n.m.r. and space-filling molecular models. The secondary structure previously established in detail in ‘dry’ dimethyl sulphoxide [Heatley, Scott & Hull (1984) Biochem. J. 220, 197-205] undergoes changes on addition of water, compatible with the incorporation of a water bridge between the uronate carboxylate and acetamido NH groups. Molecular models show that such a configuration is highly probable, and saturation-transfer experiments yield rates of NH proton exchange that support this proposed structure. The existence of two distinct stable configurations for hyaluronan, in water-rich and water-poor conditions respectively, may have biological implications, e.g. during its biosynthesis in cell membranes. There are extensive hydrophobic regions in both forms, which may be important for interactions with e.g., membranes, proteins and itself.

scholarly journals Peptide-chain secondary structure of bacteriorhodopsin

1983 ◽  
Vol 43 (1) ◽  
pp. 81-89 ◽  
Author(s):  
B.K. Jap ◽  
M.F. Maestre ◽  
S.B. Hayward ◽  
R.M. Glaeser
Keyword(s):  
Secondary Structure ◽  
Peptide Chain

Gas-Phase Folding of a Two-Residue Model Peptide Chain: On the Importance of an Interplay between Experiment and Theory

2010 ◽  
Vol 132 (34) ◽  
pp. 11860-11863 ◽  
Author(s):  
E. Gloaguen ◽  
B. de Courcy ◽  
J.-P. Piquemal ◽  
J. Pilmé ◽  
O. Parisel ◽  
...  
Keyword(s):  
Gas Phase ◽  
Peptide Chain ◽  
Model Peptide

(μ3-Benzene-1,3,5-tricarboxylato)tris[aqua(N,N,N′,N′′,N′′-pentamethyldiethylenetriamine)nickel(II)] tris(perchlorate) 4.25-hydrate

2007 ◽  
Vol 63 (11) ◽  
pp. m2860-m2861
Author(s):  
Zdeněk Trávníček ◽  
Jaromír Marek ◽  
Šárka Čermáková
Keyword(s):  
Crystal Structure ◽  
Secondary Structure ◽  
Water Molecule ◽  
Octahedral Geometry ◽  
Title Complex ◽  
Distorted Octahedral Geometry ◽  
Water Solvent ◽  
Distorted Octahedral ◽  
Intermolecular Contacts ◽  
Solvent Molecules

In the title complex, [Ni3(C9H3O6)(C9H23N3)3(H2O)3](ClO4)3·4.25H2O, the three NiII centres are bridged by a benzene-1,3,5-tricarboxylate(3−) anion (btc). Each of the metal centres is coordinated by three N atoms of a tridentate N,N,N′,N′′,N′′-pentamethyldiethylenetriamine ligand (pmdien), two O atoms of the btc ligand and one water molecule in a distorted octahedral geometry. The secondary structure is stabilized by a variety of O—H...O hydrogen bonds and C—H...O interactions that serve to connect the complex cations, perchlorate anions and water solvent molecules. Variability of intermolecular contacts stabilizing the crystal structure leads to disorder of part of O atoms of two perchlorate anions between two positions with occupancies 0.632 (5) and 0.337 (7).

Single molecule studies of surface-induced secondary structure in a model peptide

2004 ◽  
Author(s):  
Douglas S. English ◽  
Joy A. Cunningham ◽  
Sarah C. Wehri ◽  
Amy F. Petrik ◽  
Kenji Okamoto
Keyword(s):  
Secondary Structure ◽  
Single Molecule ◽  
Model Peptide ◽  
Single Molecule Studies

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

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