MI Remote・TV Box Controller vs pKaTool

Take full control of your Mi Box with the MI Remote Control app, turning your smartphone into a versatile remote. Navigate, launch apps, and manage your entertainment with ease—all from the palm of your hand! Key Features: - Complete Remote Control: Access all essential functions such as volume, power, and navigation buttons to operate your Mi Box smoothly. - App Management: Open, close, and switch between apps on your Mi Box directly from your phone with simple commands. - Voice Search: Use voice commands to quickly find your favorite shows, movies, or apps without typing. - Touchpad Navigation: Enjoy enhanced control with a built-in touchpad for precise navigation and smooth browsing. - Quick & Easy Setup: Pair your phone with your Mi Box in seconds and start managing your TV experience right away. - Multi-Device Support: Easily switch between multiple Mi Box devices if you have more than one. Disclaimer: This app is not affiliated with, endorsed by, or authorized by Xiaomi. It is an independent tool designed to enhance your control over your Mi Box device. Download now and enjoy seamless, convenient control over your Mi Box! Payment will be charged to the credit card connected to your iTunes Account when you confirm the initial subscription purchase. Subscriptions automatically renew unless auto-renew is turned off at least 24-hours before the end of the current subscription period. Your account will be charged for renewal within 24-hours prior to the end of the current period, and the cost of the renewal will be identified. You may manage your subscription and auto-renewal may be turned off by going to your Account Settings after the purchase. Any unused portion of a free trial period, if offered, will be forfeited when you purchase a subscription, where applicable. The App offers auto-renewing subscriptions to provide you with unlimited access to all features with no limits while you maintain an active subscription. Terms of Use: https://1drv.ms/w/s!AuLKRnT6jIVOa5TvWWveRZSYloY?e=5kMchd Privacy Policy: https://1drv.ms/w/s!AuLKRnT6jIVObPszqzm_FWKpqFs?e=kdpZPd

pKaTool — Titratable Groups, Made Intuitive pKaTool is a hands-on lab for exploring how acids and bases behave when they're not alone. Real proteins pack titratable groups close together in active sites, and their pKa values shift because of it — coupling that's easy to state on paper but hard to feel until you can play with it. Built for the classroom as much as the lab bench. Set up a system of titratable groups, assign each an intrinsic pKa and an acid or base identity, then adjust the pairwise interaction energy between them. pKaTool solves the exact Boltzmann partition function for every protonation state — no approximation, no Monte Carlo sampling — and redraws the titration curve live as you move the sliders. NEW: pH-activity profiles Mark which protonation state of an active site is catalytically competent, and pKaTool overlays the resulting pH-activity profile on the chart — the same calculation behind published pH-dependent enzyme activity curves. Watch how coupling between two or three residues can shift an enzyme's pH optimum by a full pH unit. NEW: Six systems from the literature Load real, published active-site electrostatics instead of only synthetic examples — intrinsic pKa values and interaction energies transcribed directly from an NMR/GloFTE study of enzyme active sites (Sondergaard et al., J. Mol. Biol. 2008), including a wild-type xylanase and its N35D mutant reproducing a published pH-activity optimum shift (5.7 to 4.6), ribonuclease A, and both oxidation states of thioredoxin. Initial version based on Analysing the pH-dependent properties of proteins using pKa calculations, Jens Erik Nielsen J Mol Graph Model. 2007 Jan;25(5):691-9. doi: 10.1016/j.jmgm.2006.05.007. https://pubmed.ncbi.nlm.nih.gov/16815056/ What you can explore: • Intrinsic pKa vs. effective pKa — watch a group's apparent pKa shift as neighboring charges turn on and off • Repulsive vs. attractive coupling, applied automatically from each group's acid/base identity, just like real electrostatics • Back-titration — the counterintuitive case where a group re-protonates partway through a titration because its neighbors' charge state changes the energetics • pH-activity profiles for enzyme active sites, and net charge and isoelectric point across your full pH range Why it's useful for teaching: • See, in real time, why two nearby acidic or basic residues almost never titrate independently — the classic Henderson-Hasselbalch curve is the special case, not the rule • Build intuition for back-titration, charge inversion, and buffering plateaus by dragging sliders instead of reading about them • Reproduce a real published figure from the primary literature, not a toy example Built for exploration: • One live screen — sliders, interaction matrix, and titration curve all update together, no "calculate" button • Save and switch between named systems to compare setups, including the six built-in literature examples • Adjustable pH scan range and resolution • No account required — systems stay on your device • Occasional non-personalized ads support development; Remove Ads turns them off Whether you're teaching enzyme active-site behavior, building intuition before a kinetics experiment, or just curious why a catalytic residue's pKa never matches the textbook value, pKaTool lets you turn the knobs yourself and watch the physics respond. Original code license: # pKaTool - analysis of systems of titratable groups # Copyright (C) 2010 Jens Erik Nielsen # # This program is free software: you can redistribute it and/or modify # it under the terms of the GNU General Public License as published by # the Free Software Foundation, either version 3 of the License, or # (at your option) any later version. # # This program is distributed in the hope that it will be useful, # but WITHOUT ANY WARRANTY; without even the implied warranty of # MERCHANTABILITY or FITNESS FOR A PARTICULAR PURPOSE. See the # GNU General Public License for more details.