Algorithm for Clustering the Moduli of RNS for the Application of Optimization of Time Complexity in Standard Cipher System

Residue number system (RNS) has emerged as a knocking field of research due to its high speed, fault tolerant, carry free and parallel characteristics. Due to these features it has got important role in high performance computing especially with reduced delay. There are various algorithms have been found as a result of the research with respect to RNS. Additionally, since RNS reduces word length due to the modular operations, its computations are faster compared to binary computations. But the major challenges are the selection of moduli sets for the forward (decimal to residue numbers) and reverse (residue numbers to decimal) conversion. RNS performance is purely depending on how efficiently an algorithm computes / chooses the moduli sets [1]-[6]. This paper proposes new method for selecting the moduli sets and its usage in cryptographic applications based on Schonhage modular factorization. The paper proposes six moduli sets {6qk1, 6qk+1, 6qk+3, 6qk+5, 6qk+7, 6qk+11} for the RNS conversions but the Schonhage moduli sets are expressed as the exponents that creates a large gap between the moduli’s computed. Hence, a new method is proposed to for computing moduli sets that helps in representing all the decomposed values approximately in the same range.

ICI and PAPR enhancement in MIMO-OFDM system using RNS coding

<p><span>The Inter-Carrier-Interference (ICI) is considered a bottleneck in the utilization of Multiple-Input-Multiple-Output Orthogonal Frequency Division Multiplexing (MIMO-OFDM) systems, due to the sensitivity of the OFDM towards frequency offsets which lead to loss of orthogonality, interference and performance degradation. In this paper Residue Numbers as a coding scheme is impeded in MIMO-OFDM systems, where the ICI levels is measured and evaluated with respect to conventional ICI mitigation techniques implemented in MIMO-OFDM. The Carrier-to-Interference Ratio (CIR), the system Bit-Error-Rate (BER) and the Complementary Cumulative Distribution Function (CCDF) for MIMO-OFDM system with Residue Number System (RNS) coding are analyzed and evaluated. The results had demonstrated a performance of transmission model with and without RNS.</span></p>

New fungal defensin-like peptides provide evidence for fold change of proteins in evolution

Defensins containing a consensus cystine framework, Cys[1]…Cys[2]X3Cys[3]…Cys[4]… Cys[5]X1Cys[6] (X, any amino acid except Cys; …, variable residue numbers), are extensively distributed in a variety of multicellular organisms (plants, fungi and invertebrates) and essentially involved in immunity as microbicidal agents. This framework is a prerequisite for forming the cysteine-stabilized α-helix and β-sheet (CSαβ) fold, in which the two invariant motifs, Cys[2]X3Cys[3]/Cys[5]X1Cys[6], are key determinants of fold formation. By using a computational genomics approach, we identified a large superfamily of fungal defensin-like peptides (fDLPs) in the phytopathogenic fungal genus – Zymoseptoria, which includes 132 structurally typical and 63 atypical members. These atypical fDLPs exhibit an altered cystine framework and accompanying fold change associated with their secondary structure elements and disulfide bridge patterns, as identified by protein structure modelling. Despite this, they definitely are homologous with the typical fDLPs in view of their precise gene structure conservation and identical precursor organization. Sequence and structural analyses combined with functional data suggest that most of Zymoseptoria fDLPs might have lost their antimicrobial activity. The present study provides a clear example of fold change in the evolution of proteins and is valuable in establishing remote homology among peptide superfamily members with different folds.

The role of N-terminal and C-terminal Arg residues from BK on interaction with kinin B2 receptor

Bradykinin (BK) is a nonapeptide important for several physiological processes such as vasodilatation, increase in vascular permeability and release of inflammatory mediators. BK performs its actions by coupling to and activating the B2 receptor, a family A G-protein coupled receptor. Using a strategy which allows systematical monitoring of BK R1 and R9 residues and B2 receptor acidic residues Glu5.35(226) and Asp6.58(298), our study aims at clarifying the BK interaction profile with the B2 receptor [receptor residue numbers are normalized according to Ballesteros and Weinstein, Methods Neurosci. 25 (1995), pp. 366–428) followed by receptor sequence numbering in brackets]. N- and C-terminal analogs of BK (-A1, -G1, -K1, -E1 and BK-A9) were tested against wild type B2, Glu5.35(226)Ala and Asp6.58(298)Ala B2 mutant receptors for their affinity and capability to elicit responses by mechanical recordings of isolated mice stomach fundus, measuring intracellular calcium mobilization, and competitive fluorimetric binding assays. BK showed 2- and 15-fold decreased potency for Glu5.35(226) and Asp6.58(298) B2 mutant receptors, respectively. In B2-Glu5.35(226)Ala BK analogs showed milder reduction in evaluated parameters. On the other hand, in the B2-Asp6.58(298)Ala mutant, no N-terminal analog was able to elicit any response. However, the BK-A9 analog presented higher affinity parameters than BK in the latter mutant. These findings provide enough support for defining a novel interaction role of BK-R9 and Asp6.58(298) receptor residues.