Glossary
- Page ID
- 398297
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\(\newcommand{\avec}{\mathbf a}\) \(\newcommand{\bvec}{\mathbf b}\) \(\newcommand{\cvec}{\mathbf c}\) \(\newcommand{\dvec}{\mathbf d}\) \(\newcommand{\dtil}{\widetilde{\mathbf d}}\) \(\newcommand{\evec}{\mathbf e}\) \(\newcommand{\fvec}{\mathbf f}\) \(\newcommand{\nvec}{\mathbf n}\) \(\newcommand{\pvec}{\mathbf p}\) \(\newcommand{\qvec}{\mathbf q}\) \(\newcommand{\svec}{\mathbf s}\) \(\newcommand{\tvec}{\mathbf t}\) \(\newcommand{\uvec}{\mathbf u}\) \(\newcommand{\vvec}{\mathbf v}\) \(\newcommand{\wvec}{\mathbf w}\) \(\newcommand{\xvec}{\mathbf x}\) \(\newcommand{\yvec}{\mathbf y}\) \(\newcommand{\zvec}{\mathbf z}\) \(\newcommand{\rvec}{\mathbf r}\) \(\newcommand{\mvec}{\mathbf m}\) \(\newcommand{\zerovec}{\mathbf 0}\) \(\newcommand{\onevec}{\mathbf 1}\) \(\newcommand{\real}{\mathbb R}\) \(\newcommand{\twovec}[2]{\left[\begin{array}{r}#1 \\ #2 \end{array}\right]}\) \(\newcommand{\ctwovec}[2]{\left[\begin{array}{c}#1 \\ #2 \end{array}\right]}\) \(\newcommand{\threevec}[3]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \end{array}\right]}\) \(\newcommand{\cthreevec}[3]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \end{array}\right]}\) \(\newcommand{\fourvec}[4]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \\ #4 \end{array}\right]}\) \(\newcommand{\cfourvec}[4]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \\ #4 \end{array}\right]}\) \(\newcommand{\fivevec}[5]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \\ #4 \\ #5 \\ \end{array}\right]}\) \(\newcommand{\cfivevec}[5]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \\ #4 \\ #5 \\ \end{array}\right]}\) \(\newcommand{\mattwo}[4]{\left[\begin{array}{rr}#1 \amp #2 \\ #3 \amp #4 \\ \end{array}\right]}\) \(\newcommand{\laspan}[1]{\text{Span}\{#1\}}\) \(\newcommand{\bcal}{\cal B}\) \(\newcommand{\ccal}{\cal C}\) \(\newcommand{\scal}{\cal S}\) \(\newcommand{\wcal}{\cal W}\) \(\newcommand{\ecal}{\cal E}\) \(\newcommand{\coords}[2]{\left\{#1\right\}_{#2}}\) \(\newcommand{\gray}[1]{\color{gray}{#1}}\) \(\newcommand{\lgray}[1]{\color{lightgray}{#1}}\) \(\newcommand{\rank}{\operatorname{rank}}\) \(\newcommand{\row}{\text{Row}}\) \(\newcommand{\col}{\text{Col}}\) \(\renewcommand{\row}{\text{Row}}\) \(\newcommand{\nul}{\text{Nul}}\) \(\newcommand{\var}{\text{Var}}\) \(\newcommand{\corr}{\text{corr}}\) \(\newcommand{\len}[1]{\left|#1\right|}\) \(\newcommand{\bbar}{\overline{\bvec}}\) \(\newcommand{\bhat}{\widehat{\bvec}}\) \(\newcommand{\bperp}{\bvec^\perp}\) \(\newcommand{\xhat}{\widehat{\xvec}}\) \(\newcommand{\vhat}{\widehat{\vvec}}\) \(\newcommand{\uhat}{\widehat{\uvec}}\) \(\newcommand{\what}{\widehat{\wvec}}\) \(\newcommand{\Sighat}{\widehat{\Sigma}}\) \(\newcommand{\lt}{<}\) \(\newcommand{\gt}{>}\) \(\newcommand{\amp}{&}\) \(\definecolor{fillinmathshade}{gray}{0.9}\)Words (or words that have the same definition) | The definition is case sensitive | (Optional) Image to display with the definition [Not displayed in Glossary, only in pop-up on pages] | (Optional) Caption for Image | (Optional) External or Internal Link | (Optional) Source for Definition |
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(Eg. "Genetic, Hereditary, DNA ...") | (Eg. "Relating to genes or heredity") | ![]() | The infamous double helix | https://bio.libretexts.org/ | CC-BY-SA; Delmar Larsen |
Word(s) | Definition | Image | Caption | Link | Source |
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Thermodynamic Variables | Quantities that define the state of a system (e.g., pressure, volume, temperature, and chemical composition). | ||||
Equations of State | Mathematical relationships that describe the state of a system, such as the ideal gas law. | ||||
First Law of Thermodynamics | Law of energy conservation, stating that energy cannot be created or destroyed, only transformed. | ||||
Thermochemistry | Study of heat changes that occur during chemical reactions. | ||||
Second Law of Thermodynamics | States that the total entropy of an isolated system always increases over time. | ||||
Boltzmann Distribution | Describes the distribution of particles among available energy states in a system. | ||||
Statistical Definition of Entropy | Entropy is related to the number of possible microstates in a system, quantified by the Boltzmann constant. | ||||
Gibbs Free Energy | A thermodynamic potential used to predict the spontaneity of a process at constant temperature and pressure. | ||||
Helmholtz Free Energy | A thermodynamic potential used to predict spontaneity at constant temperature and volume. | ||||
Equilibria in Biochemical Systems | Describes the balance between forward and reverse reactions in biochemical processes. | ||||
Kinetic Rate Laws | Mathematical expressions that describe the rate of a chemical reaction as a function of reactant concentrations. | ||||
Reaction Mechanisms | A step-by-step sequence of elementary reactions that leads to the overall chemical transformation. | ||||
Transition State Theory | Theory that explains how chemical reactions occur by describing the transition between reactants and products via a high-energy state. | ||||
Potential Energy Surface | A multidimensional surface that describes the energy of a system in relation to the positions of the atoms. | ||||
Bonding Interactions | Forces that hold atoms together within molecules (e.g., covalent, ionic, or hydrogen bonds). | ||||
Intermolecular Forces | Forces that act between molecules, including van der Waals forces, dipole-dipole interactions, and hydrogen bonds. | ||||
Newtonian Mechanics | A branch of physics that describes the motion of objects based on forces acting on them. | ||||
Molecular Dynamics Simulations | Computational simulations that model the behavior of atoms and molecules over time. | ||||
Analysis of Molecular Dynamics Trajectories | The process of interpreting the results from molecular dynamics simulations to understand molecular behavior. | ||||
Advanced Topics in Molecular Dynamics | In-depth concepts like enhanced sampling techniques, free energy calculations, and multiscale modeling. | ||||
Spectroscopy | The study of the interaction between matter and electromagnetic radiation. | ||||
Basic Elements of Spectroscopy | Components such as light sources, detectors, and sample cells used in spectroscopic analysis. | ||||
Two Masses on a Spring Model | A simplified model used to describe molecular vibrations, particularly relevant in infrared (IR) spectroscopy. | ||||
Infrared (IR) Spectroscopy | A technique that measures the absorption of infrared light by molecules, helping identify functional groups. | ||||
Quantum Mechanics and Quantum Oscillator Model | Describes molecular vibrations and energy levels as quantized. | ||||
Fluorescence | The emission of light by a molecule that has absorbed light or other electromagnetic radiation. | ||||
Phosphorescence | Emission of light from a molecule following absorption, where the emission persists longer than fluorescence. | ||||
Nuclear Spin | The intrinsic angular momentum of nuclei that can interact with magnetic fields. | ||||
Magnetic Field | A field that affects the behavior of magnetic dipoles like nuclear spins, fundamental to NMR spectroscopy. | ||||
Excite-Record Experiment | The process of exciting nuclei with a magnetic pulse and recording their response to generate an NMR spectrum. | ||||
Chemical Shift | The displacement of a resonance frequency relative to a standard, measured in parts per million (ppm). | ||||
Fourier Transformation, FT | A mathematical method to convert data from the time domain (FID) into the frequency domain (NMR spectrum). | ||||
Spectral Sensitivity and Resolution | Factors that determine the clarity and detail of an NMR spectrum, influenced by the sample, equipment, and experimental conditions. | ||||
2D NMR Spectroscopy | A technique that provides information on atomic interactions in a protein, allowing higher spectral resolution and better peak assignment. | ||||
Heteronuclear 3D NMR | A three-dimensional NMR technique that involves multiple types of nuclei, enabling resonance assignments and structural analysis of proteins. | ||||
Protein Dynamics | The study of how proteins change shape and function in response to their environment, often analyzed through NMR. | ||||
Conformational States | Different shapes that a protein can adopt, which can influence its biological activity. | ||||
NMR for Protein Function | Using NMR spectroscopy to understand how protein structure relates to its biological function and dynamics. |