ABSTRACT
Calculating forward and inverse kinematics for robotic agents is one of the most time-intensive tasks when controlling the robot movement in any environment. This calculation is then encoded to control the motors and validated in a simulator. The feedback produced by the simulation can be used to correct the code or to implement the code can be implemented directly in the robotic agent. However, the simulation process executes instructions that are not native to the robotic agents, extending development time or making it preferable to validate the code directly on the robot, which in some cases might result in severe damage to it. The use of Domain-Specific Languages help reduce development time in simulation tasks. These languages simplify code generation by describing tasks through an easy-to-understand language and free the user to use a framework or programming API directly for testing purposes. This article presents the language PyDSLRep, which is characterized by the connection and manipulation of movement in mobile robotic agents in the V-Rep simulation environment. This language is tested in three different environments by twenty people, against the framework given by V-Rep, demonstrating that PyDSLRep reduces the average development time by 45.22%, and the lines of code by 76.40% against the Python framework of V-Rep.
Subject(s)
Programming Languages , Robotics/methods , Biomechanical Phenomena , Computer Simulation , Equipment Design , Humans , Movement , Robotics/instrumentationABSTRACT
The mechanisms of exercise-induced fatigue have not been investigated using proteomic techniques, an approach that could improve our understanding and generate novel information regarding the effects of exercise. In this study, the proteom alterations of rat skeletal muscle were investigated during exercise-induced fatigue. The proteins were extracted from the skeletal muscle of SD rat thigh, and then analyzed by two-dimensional electrophoresis and PDQuest software. Compared to control samples, 10 significantly altered proteins were found in exercise samples, two of them were upregulated and eight of them were downregulated. These proteins were identified by MALDI TOF-MS. The two upregulated proteins were identified as MLC1 and myosin L2 (DTNB) regulatory light-chain precursors. The eight decreased proteins are Glyceraldehyde-3-phosphate Dehydrogenas (GAPDH); Beta enolase; Creatine kinase M chain (M-CK); ATP-AMP Transphosphorylase (AK1); myosin heavy chain (MHC); actin; Troponin I, fast-skeletal muscle (Troponin I fast-twitch isoform), fsTnI; Troponin T, fast-skeletal muscle isoforms (TnTF). In these proteins, four of the eight decreased proteins are related directly or indirectly to exercise induced fatigue. The other proteins represent diverse sets of proteins including enzymyes related to energy metabolism, skeletal muscle fabric protein and protein with unknown functions. They did not exhibit evident relationship with exercise-induced fatigue. Whereas the two identified increased proteins exhibit evident relationship with fatigue. These findings will help in understanding the mechanisms involved in exercise-induced fatigue.
Subject(s)
Muscle Fatigue/physiology , Muscle Proteins/metabolism , Muscle, Skeletal/metabolism , Physical Exertion/physiology , Animals , Body Weight/physiology , Electrophoresis, Gel, Two-Dimensional , Energy Metabolism/physiology , Male , Mass Spectrometry , Models, Animal , Muscle Proteins/chemistry , Proteomics , Random Allocation , Rats , Rats, Sprague-Dawley , Swimming/physiology , Troponin I/chemistry , Troponin I/metabolism , Troponin T/chemistry , Troponin T/metabolismABSTRACT
The mechanisms of exercise-induced fatigue have not been investigated using proteomic techniques, an approach that could improve our understanding and generate novel information regarding the effects of exercise. In this study, the proteom alterations of rat skeletal muscle were investigated during exercise-induced fatigue. The proteins were extracted from the skeletal muscle of SD rat thigh, and then analyzed by two-dimensional electrophoresis and PDQuest software. Compared to control samples, 10 significantly altered proteins were found in exercise samples, two of them were upregulated and eight of them were downregulated. These proteins were identified by MALDI TOF-MS. The two upregulated proteins were identified as MLC1 and myosin L2 (DTNB) regulatory light-chain precursors. The eight decreased proteins are Glyceraldehyde-3-phosphate Dehydrogenas (GAPDH); Beta enolase; Creatine kinase M chain (M-CK); ATP-AMP Transphosphorylase (AK1); myosin heavy chain (MHC); actin; Troponin I, fast-skeletal muscle (Troponin I fast-twitch isoform), fsTnI; Troponin T, fast-skeletal muscle isoforms (TnTF). In these proteins, four of the eight decreased proteins are related directly or indirectly to exercise induced fatigue. The other proteins represent diverse sets of proteins including enzymyes related to energy metabolism, skeletal muscle fabric protein and protein with unknown functions. They did not exhibit evident relationship with exercise-induced fatigue. Whereas the two identified increased proteins exhibit evident relationship with fatigue. These findings will help in understanding the mechanisms involved in exercise-induced fatigue.