it's an IB style design part of a biology lab report about beetrootFull description
The effect of different temperature of homogeneous mixture consisting of distilled water and Agaricus bisporus on enzyme activity.Full description
The effect of different concentrations of blackcurrant squash on the rate of osmosis in Solanum tuberosum.
All living things are made up of cells, including humans, animals and plants. Every cell’s purpose is to survive for them to perform their function well. This laboratory experiment is limited only ...
2.1 Cell Structure & FunctionFull description
LBYBIOJ Pre-Midterm Review Dilution Factor = total volume/volume sample Beer’s Law — relationship between concentration and the amount of light the sample absorbs High Concentration : High Absorbance Why should colorimetric assays be read at wavelength of maximum absorption? ( !max) Wavelength — crest to crest Shorter Wavelength — more energetic (e.g. x-rays 50-100 nm) Long Wavelengths — less energetic (!max) — can — can easily distinguish one concentration to from another What is the mechanism behind the Bradford Assay? The Bradford Assay 1. dye non-covalently binds (hydrophobic and electrostatic) to protein 2. stabilizes —> lower energy 3. spectral properties change (changes to blue) 4. since electrostatic bonds, when pH changes, the binging changes (change colors)
3 Forms of Bradford 1. Cationic (very low pH=470 nm) RED 2. Neutral (low pH=650 nm) GREEN 3. Anionic (low-mid pH=595 nm) BLUE Differentiate Coomassie G-250 & R-250. R-250 — R-250 — R for slightly reddish tint — can be used to detect as little as 0.1 µg of protein — lacks two methyl groups present in G-250 G-250 — G for slightly greenish tint — “colloidal Coomassie dye” — requires faster staining protocol — reacts with proteins and not with gel What are other colorimetric methods for protein analysis? Biuret Test — colavently bonding, Cu+ chaltes with proteins at carbonyl O2 (sp2 hybridized) —disregards shape and composition of protein —two different proteins at same concentrations would have the same intensity Bradford Test — non-covalent, shape-dependent What are the factors affecting Colorimetric Protein Analysis
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shape composition pH temperature Grinding Buffer — maintains the osmolarity in the environment Density — basis of separation
Other Methods of Homogenization • Blender • Homogenizer • Sonication • Freeze-throw cycle • Mortar and Pestle SDS-PAGE Basis of Separation — Molecular Weight and Size Sodium Dodecyl Sulfate — denatures the protein, gives uniform negative charge, uniform shape 110 — Average molecular weight of an amino acid Boiling — denatures protein, non-covalent bonds destroyed due to high kinetic energy 2-mercaptoethanol — destroys the disulfide linkages Homology Modelling — useful when there is no experimental data 3D structures : X-ray Crystallography and NMR template — basis for structure Criteria: if protein is mutant, use wild type; if protein is not mutant, use protein family Non-covalent Interactions Salt Birdges — electrostatic interaction Ramachandran Plot — description of the 3D structure psi — alpha carbon and carbonyl phy — alpha arbon and nitrogen Partial Double Bond Character — characteristic of the Omega Angle, not considered in Rama
C1V1 = C2V2 ** make sure same unit of measurement for all **dilution factor Alkaline Phosphadiesterase Assay
