Cell adhesion molecules are important for their various roles in many cellular events and responses. In the present study, we have analyzed the roles played by cation-π interactions in the structural stability of adhesion molecules. These interactions are mainly formed by long-range contacts. The occurrence of arginine is higher than lysine to form cation-π interactions. The secondary structure preferences of interacting residues are independent of amino acid class. Cation-π interactions might stabilize the interface between the terminus and core in this class of proteins. The results obtained in the present study will be useful in understanding the contribution of cation-π interactions to the overall stability of adhesion proteins. © 2010 Springer-Verlag.

Anand A

Department of Biotechnology

School of Bio Sciences and Technology

Vellore Campus

Sophiya K

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Protoplasma

p-p Interactions play an important role in the stability of protein structures. In the present study, we have analyzed the influence of p-p interactions in eNOS and nNOS proteins. The contribution of these p-p interacting residues in sequential separation, secondary structure involvement, solvent accessibility and stabilization centers has been evaluated. p-p interactions stabilize the core regions within eNOS and nNOS proteins. p-p interacting residues are evolutionary conserved. There is a significant number of p-p interactions in spite of the lesser natural occurrences of p-residues in eNOS and nNOS proteins. In addition to p-p interactions, presidues also form p-p networks in both eNOS and nNOS proteins which might play an important role in the structural stability of these protein structures. © 2013 Elsevier Inc. All rights reserved.

Bioorganic Chemistry

Investigations on the role of π–π interactions and π–π networks in eNOS and nNOS proteins

β-lactam group of antibiotics is the most widely used therapeutic molecules for treating bacterial infections. The main mode of bacterial resistance to β-lactams is by β-lactamases. In the present study, we report our results on the role of cation-π interactions in β-lactamases and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while tyrosine is comparatively higher than phenylalanine and tryptophan in the π group. Our results indicate that cation-π interactions might play an important role in the global conformational stability of β-lactamases.

Cell Biochemistry and Biophysics

Cation–π Interactions in β-Lactamases: The Role in Structural Stability

Fulltext

Bioinformation

Arginine and Lysine interactions with p residues in metalloproteins

We have analyzed and compared the influence of cation-π interactions in glycoproteins (GPs), lipid-binding proteins (LBPs) and RNA-binding proteins (RBPs) in this study. We observed that all the proteins included in the study had profound cation-π interactions. There is an average of one energetically significant cation-π interaction for every 71 residues in GPs, for every 58 residues in LBPs and for every 64 residues in RBPs. Long-range contacts are predominant in all the three types of proteins studied. The pair-wise cation-π interaction energy between the positively charged and aromatic residues shows that Arg-Trp pair energy was the strongest among all six possible pairs in all the three types of proteins studied. There were considerable differences in the preference of cation-π interacting residues to different secondary structure elements and ASA and these might contribute to differences in biochemical functions of GPs, LBPs and RBPs. It was interesting to note that all the five residues involved in cation-π interactions were found to have stabilization centers in GPs, LBPs and RBPs. Majority of the cation-π interacting residues investigated in the present study had a conservation score of ≥6, the cutoff value used to identify the stabilizing residues. A small percentage of cation-π interacting residues were also present as stabilizing residues. The cation-π interaction-forming residues play an important role in the structural stability of in GPs, LBPs and RBPs. The results obtained in this study will be helpful in further understanding the stability, specificity and differences in the biochemical functions of GPs, LBPs and RBPs. © 2007 Elsevier Ltd. All rights reserved.

Journal of Theoretical Biology

Exploring the role of cation–π interactions in glycoproteins lipid-binding proteins and RNA-binding proteins

Journal of Molecular Modeling

A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure

Journal of Molecular Biology

Energetics of Protein Folding

Advances in Enzymology - and Related Areas of Molecular Biology,Advances in Enzymology and Related Areas of Molecular Biology

Prediction of the Secondary Structure of Proteins from their Amino Acid Sequence

Proceedings of the National Academy of Sciences

A backbone-based theory of protein folding

Structural stability studies in adhesion molecules—role of cation–π interactions

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Publisher	Data powered by TypesetSpringer Science and Business Media LLC
ISSN	0033-183X
Open Access	0