190 research outputs found
Wireless Security System with Password Protection
Home security is not minor issue because crime is increasing and everyone wants to take proper measures to prevent invasion [1]. In this paper, design and implement of a microcontroller based wireless security system with password protection have been presented and analyzed. Microcontrollers with other peripheral devices which include Liquid Crystal Display (LCD), Buzzer, Sensors, Encoder and RF Module are responsible for reliable operation of the proposed security system. In addition, the system is provided with a manual keypad which provides a password protection in order to provide extra security to the system. Assembly language is used as the programming language and Atmel is used to compile the code in order to design a program that controls the system along with maintaining all security functions
Founding properties on non-ferrous liquid metals
ALTHOUGH the liquid state is the first step of all founding operations no fundamental measure is available
to evaluate the capacity of liquid metals to flow adeq-uately into intricate moulds. Whilst a consideration of viscosity & surface tension is natural in any discussion of the flow of liquid metals, it is not adequate to describe their founding characteristics.In this paper an attempt has been made to evolve a fundamental basis of viscosity and surface tension and their impact on casting fluidity
DBRS: Directed Acyclic Graph based Reliable Scheduling Approach in Large Scale Computing
In large scale environments, scheduling presents a significant challenge because it is an NP-hard problem. There are basically two types of task in execution- dependent task and independent task. The execution of dependent task must follow a strict order because output of one activity is typically the input of another. In this paper, a reliable fault tolerant approach is proposed for scheduling of dependent task in large scale computing environments. The workflow of dependent task is represented with the help of a DAG (directed acyclic graph). The proposed methodology is evaluated over various parameters by applying it in a large scale computing environment- ‘grid computing’. Grid computing is a high performance computing for solving complex, large and data intensive problems in various fields. The result analysis shows that the proposed DAG based reliable scheduling (DBRS) approach increases the performance of system by decreasing the makespan, number of failures and increasing performance improvement ratio (PIR)
Agent Based Software Testing for Multi Agent Systems
Software testing starts with verification and validation and fulfills the requirement of the customer. Testing can be done by automation tool like Win runner, QTP or manually. If we talk about manual testing it takes lot of time and manpower also so nowadays we are using automation software. When we talk about automation testing so the cost of such kind of testing is very high so each company cannot afford. In this paper we are presenting agent based testing which is helpful for both kind of testing. Multi-Agent Systems (MAS) are characterized by autonomous and collaborative behaviors [1, 2]. Developing such systems is a complex process. As a result, a methodology for developing MAS is highly necessary. In this paper, a methodology using roles and ontology for such a purpose is presented [2]. The functionality of roles is estimated in the various phases of the MAS development. It is based on an emphasis on the properties and behaviors associated with each agent in MAS
Proximally migrated Double J stent in hydronephrotic kidneys: Etiological factors and management
Double J stents have become an essential tool in urologist’s armamentarium but are never without potential complications. Migration of DJ stent is a recognized complication, though its proximal migration into the upper ureter, pelvicalyceal system is reported rarely. This can add to the cost of patients and increases hospital stay if another general/ regional anesthesia session is required for its repositioning/removal. We successfully repositioned or removed proximally migrated DJ stents ureteroscopically under local anesthesia and analgesia in all of our case series patients on a daycare basis. We emphasize the importance of recordkeeping and follow up of stented patients particularly with those with hydronephrotic systems. In the event of proximal migration of the DJ stent, it can be successfully repositioned or removed under local anesthesia and analgesia.
Keywords: Double J stent, proximal migration, ESWL-Extracorporeal shockwave lithotrips
The many faces of amyloid fibres: their detection and regulation by molecular chaperone proteins
Proteins are the molecular machines that control and regulate
most of the vital cellular functions in living organisms, and
account for about half of the total dry mass of the cell. For a
protein to function properly, it must attain its correct
conformation and location within the crowded milieu of the cell.
A complex set of molecular chaperone proteins assist polypeptides
to acquire their native functional fold within the relevant
biological timescale. However, the intricacy and diverse nature
of the protein folding process and various environmental factors
present numerous opportunities for error, which may lead to its
misfolding and aggregation. Misfolded, aggregated, non-functional
proteins and peptides within the cell are implicated with more
than 55 pathological conditions including various
neurodegenerative diseases such as Alzheimer’s,Parkinson’s
and haemodialysis-related amyloidosis, which together affect more
than 24 million people worldwide. Collectively, these disorders
are classified as protein conformational or protein aggregation
diseases. Over the past few years, significant progress has been
made to understand the various types and processes of protein
aggregation, identify the toxic species, structurally
characterise various species generated during their assembly and
comprehend the underlying mechanisms which regulate protein
conformational diseases. This thesis has attempted to address
some of the issues discussed above, to assist in advancing the
understanding of the complexities of protein misfolding,
aggregation and their mitigation.
In this thesis, I have found that various fragments of mouse Acyl
co-enzyme thioesterase 7 (mAcot7) and human full-length ACOT7
form amyloid fibrils under physiological conditions. Acot7 is a
brain cytosolic protein, involved in fatty acid metabolism, and
has a putative role during inflammation. Using various mouse
Acot7 constructs, I demonstrated that mAcot7 undergoes
nucleation-independent, multi-stranded polymerisation, leading to
the formation of globular oligomeric species and subsequently
amyloid fibrils. Arachidonoyl-CoA, the substrate of mAcot7 did
not prevent the fibrillation of mAoct7, and the protein remained
enzymatically active throughout the assembly process.
Understanding the biological significance of fibrillar and other
forms of Acot7 is one of the avenues to be explored in the
future.
After putting forth a unique molecular model of mouse Acot7
fibrillation, the next objective was to identify and characterise
the heterogeneous population of protein aggregates formed during
polymerisation. Bis(Triphenylphosphonium) tetraphenylethene
(TPE-TPP), a novel aggregation-induced emission luminogen aided
in detecting early-stage protein aggregates; the species that are
considered to be the most toxic entities during the development
and progression of protein conformational diseases. Compared to
traditional amyloid binding fluorescent dyes such as Thioflavin T
(ThT), TPE-TPP showed a broader applicability in monitoring the
process of fibrillation in various conditions such as acidic pH,
elevated temperature, presence of potential amyloid inhibitors,
and its ability to detect variations in amyloid fibril
morphologies.
Once I could differentiate between the different species
generated during protein aggregation, I attempted to explore ways
to modify these entities. Utilising the intra- and extra-cellular
molecular chaperones αB-crystallin (αB-C), clusterin,
α2-macroglobulin and haptoglobin, I observed that αB-C and
clusterin stabilise various forms of D76N β2-microglobulin (a
potent amyloidogenic variant of β2-microglobulin) generated
during the fibrillation process. It is likely that these
chaperones prevent primary and secondary nucleation of D76N
β2-microglobulin (D76N β2m) fibrillation in vivo and decelerate
the proliferation of amyloid fibril plaques.
Experiments performed in vitro are usually less confined compared
to the crowded cellular environment, and such crowding conditions
further confound the process of protein aggregation. Moreover,
oligomers of various amyloid proteins such as α-synuclein (αS)
are believed to be the primary cause of cellular damage, for
example in Parkinson’s disease. Utilising the highly identical
presynaptic α- and β-synuclein and crowding agents such as
Ficoll 400, I analysed the impact of crowding on the association
of the synuclein proteins. Under physiologically relevant
conditions, I found that β-synuclein (βS) exists as positively
charged oligomers, which gradually polymerise to form
self-assembled, non-amyloid fibril-like structures. Furthermore,
βS destabilises αS and induces its aggregation, which is
significantly moderated under the crowded cell-like environment.
The results documented in this dissertation have assisted in
advancing our knowledge and understanding of the molecular,
biophysical and biochemical mechanisms of amyloid fibril
formation. In addition, this thesis determined the broader
applicability of TPE-TPP compared to the standard amyloid dye
(i.e. ThT) as a fluorescent probe to monitor amyloid fibril
formation, detect early-stage aggregates, variations in fibril
morphologies, and can be deemed useful in screening amyloid
inhibitors. Part of the aim to identify and characterise various
protein aggregate species was to develop a method for regulating
potentially toxic entities. I showed that intra- and
extra-cellular molecular chaperones were capable of acting on
different stages of D76N β2m aggregation, thereby reducing the
effects of undesirable, misfolded toxic protein forms.
Furthermore, I demonstrated that there could be other potentially
hazardous forms of unwanted protein aggregates (i.e. βS
self-assembled structures) that are not necessarily amyloid
fibrils.
Greater comprehension of protein aggregation will not only shed
light on protein conformational disorders and aid in the
development of therapeutics against their toxic effects, but may
also offer insights into opportunities for exploiting stable,
non-toxic protein conformations to our advantage
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