Do guanidinium and tetrapropylammonium ions specifically interact with aromatic amino acid side chains?
نویسندگان
چکیده
منابع مشابه
Do guanidinium and tetrapropylammonium ions specifically interact with aromatic amino acid side chains?
Many ions are known to affect the activity, stability, and structural integrity of proteins. Although this effect can be generally attributed to ion-induced changes in forces that govern protein folding, delineating the underlying mechanism of action still remains challenging because it requires assessment of all relevant interactions, such as ion-protein, ion-water, and ion-ion interactions. H...
متن کاملA study of aromatic hydrogen bonds of peptides with aromatic amino acid side-chains.
The importance of hydrogen bonding studies lies in their structural, biological and medicinal applications. Non-conventional hydrogen bonds are weak, but are found to play an important role in biological molecules. In view of their importance,a study of the aromatic hydrogen bonds in peptides with aromatic amino acid side chains was carried out. The results indicate a reasonable probability for...
متن کاملSpecificity of ion-protein interactions: complementary and competitive effects of tetrapropylammonium, guanidinium, sulfate, and chloride ions.
The interactions of ions with a model peptide (a single melittin alpha-helix) in solutions of tetrapropylammonium sulfate or guanidinium chloride were examined by molecular dynamics simulations. The tetrapropylammonium cation shares the geometrical property of essentially flat faces with the previously examined guanidinium cation, and it was found that that this geometry leads to a strong prefe...
متن کاملDo antibodies recognize amino acid side chains of protein antigens independently of the carbon backbone?
In an effort to understand the structural basis for antigen mimicry by internal image antibodies, we determined the variable (V) region sequences of two mouse mAbs that mimic the rabbit Ig a1 allotype. The results showed that while the mAb light chains did not contain any allotype-related residues, both heavy chain V regions contained within complementarity-determining region 2 an unusual seque...
متن کاملStatistically Based Reduced Representation of Amino Acid Side Chains
Preferred conformations of amino acid side chains have been well established through statistically obtained rotamer libraries. Typically, these provide bond torsion angles allowing a side chain to be traced atom by atom. In cases where it is desirable to reduce the complexity of a protein representation or prediction, fixing all side-chain atoms may prove unwieldy. Therefore, we introduce a gen...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2017
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1618071114