Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2013 Apr 30;9(8):432-9.
doi: 10.6026/97320630009432. Print 2013.

Aromatic-aromatic interactions: analysis of π-π interactions in interleukins and TNF proteins

Vaideeswaran Sivasakthi  1 , Parimelzaghan Anitha, Kalavathi Murugan Kumar, Susmita Bag, Padmanaban Senthilvel, Pandian Lavanya, Rayapadi Swetha, Anand Anbarasu, Sudha Ramaiah
Affiliations

Aromatic-aromatic interactions: analysis of π-π interactions in interleukins and TNF proteins

Vaideeswaran Sivasakthi et al. Bioinformation. .

Abstract

Aromatic-aromatic hydrogen bonds are important in many areas of chemistry, biology and materials science. In this study we have analyzed the roles played by the π-π interactions in interleukins (ILs) and tumor necrosis factor (TNF) proteins. Majority of π-π interacting residues are conserved in ILs and TNF proteins. The accessible surface area calculations in these proteins reveal that these interactions might be important in stabilizing the inner core regions of these proteins. In addition to π-π interactions, the aromatic residues also form π-networks in ILs and TNF proteins. The results obtained in the present study indicate that π-π interactions and π-π networks play important roles in the structural stability of ILs and TNF proteins.

Keywords: ILs; TNF proteins; stability; structure; π-network; π-π interactions.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Preference of π-π interacting residues in ILs and TNF proteins.
Figure 2
Figure 2
Secondary structure preferences of proteins A) Structural preferences of π-π interacting residues in ILs; B) Structural perferences of residues in TNF Proteins.
Figure 3
Figure 3
A) Conservation score of π-π interacting residues in ILs and TNF proteins; B) Conservation pattern of ILS [PDB ID 1116] using PyMol.
Figure 4
Figure 4
Stabilization centers of π-π interacting residues in ILs and TNF proteins
Figure 5
Figure 5
A) Solvent accessibility patterns of π-π interacting residues in ILs; B) Solvent accessibility patterns of π-π interacting residues in TNF proteins.
Figure 6
Figure 6
Preferential distance (in A) of π-π interacting residues in ILS and TNF proteins
Figure 7
Figure 7
A) 3π, 4π and 7π- -networks in ILS and TNF proteins; B) PyMol view of Trp-Phe interacting pairs in ILs [PDB ID 1116]; C) The PyMol view of 7π network in ILs [PDB ID 1F45].
Figure 8
Figure 8
Sequential distances of interacting pairs in ILs and TNF proteins.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

References

    1. CG Claessens, Stoddart JF. J Phys Org Chem. 1997;10:254.
    1. Fyfe MCT, Stoddart JF. Acc Chem Res. 1997;30:393.
    1. Kannan N, Vishveshwara S. Protein Eng. 2000;13:753. - PubMed
    1. Burley SK, Petsko GA. Adv Protein Chem. 1988;39:125. - PubMed
    1. Samanta U, et al. Proteins. 2000;38:288. - PubMed

LinkOut - more resources