Abstract: Orthogonal Frequency Division Multiplexing
(OFDM) is an efficient method of data transmission for high speed
communication systems. However, the main drawback of OFDM
systems is that, it suffers from the problem of high Peak-to-Average
Power Ratio (PAPR) which causes inefficient use of the High Power
Amplifier and could limit transmission efficiency. OFDM consist of
large number of independent subcarriers, as a result of which the
amplitude of such a signal can have high peak values. In this paper,
we propose an effective reduction scheme that combines DCT and
SLM techniques. The scheme is composed of the DCT followed by
the SLM using the Riemann matrix to obtain phase sequences for the
SLM technique. The simulation results show PAPR can be greatly
reduced by applying the proposed scheme. In comparison with
OFDM, while OFDM had high values of PAPR –about 10.4dB our
proposed method achieved about 4.7dB reduction of the PAPR with
low complexities computation. This approach also avoids
randomness in phase sequence selection, which makes it simpler to
decode at the receiver. As an added benefit, the matrices can be
generated at the receiver end to obtain the data signal and hence it is
not required to transmit side information (SI).
Abstract: An alarming emergence of multidrug-resistant strains
of the tuberculosis pathogen Mycobacterium tuberculosis and
continuing high worldwide incidence of tuberculosis has invigorated
the search for novel drug targets. The enzyme glutamate racemase
(MurI) in bacteria catalyzes the stereoconversion of L-glutamate to
D-glutamate which is a component of the peptidoglycan cell wall of
the bacterium. The inhibitors targeted against MurI from several
bacterial species have been patented and are advocated as promising
antibacterial agents. However there are none available against MurI
from Mycobacterium tuberculosis, due to the lack of its threedimensional
structure. This work accomplished two major objectives.
First, the tertiary structure of MtMurI was deduced computationally
through homology modeling using the templates from bacterial
homologues. It is speculated that like in other Gram-positive bacteria,
MtMurI exists as a dimer and many of the protein interactions at the
dimer interface are also conserved. Second, potent candidate
inhibitors against MtMurI were identified through docking against
already known inhibitors in other organisms.
Abstract: Biologically active peptides are of particular interest
in food science and human nutrition because they have been shown to play several physiological roles. In vitro gastrointestinal digestion of lentil and whey proteins in this study produced high angiotensin-I converting enzyme inhibitory activity with 75.5±1.9 and 91.4±2.3%
inhibition, respectively. High ACE inhibitory activity was observed in lentil after 5 days of germination (84.3±1.2%). Fractionation by
reverse phase chromatography gave inhibitory activities as high as
86.3±2.0 for lentil, 94.8±1.8% for whey and 93.7±1.7% at 5th day of germination. Further purification by HPLC resulted in several
inhibitory peptides with IC50 values ranging from 0.064 to 0.164
mg/ml. These results demonstrate that lentil proteins are a good
source of peptides with ACE inhibitory activity that can be released by germination or gastrointestinal digestion. Despite the lower bioactivity in comparison with whey proteins, incorporation of lentil proteins in functional food formulations and natural drugs look promising.