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It returns to its original shape, and is reused. Look up the 'lock and key' and 'induced fit' models.
when models chave been validated with evidence
models are the answer
Some limitations of models are not to change what the model is asking you.
Scientist use models to study things because models are sometimes easier to use than trying to study things in a natural environment.
* Binding pedal linkage * Binding carburetor linkage (carb models) * Binding throttle body linkage or butterfly (fuel-injection models)
Choose two of the models that illustrate the stages of grief following a bereavement and compare their features to identify the similarities and differences
cimate modlesconceptual models
Office Depot carries a variety of comb style binding machines, punch binding machines, and a uni-binding machine. Some models are manual, and others are automated.
in France - approximately in 1940. see http://www.bindingstuff.net/combbinding.html for current models of comb binding equipment
Fellowes makes the full spectrum of binding machines from plastic comb binding machines to the professional thermal models. The plastic comb binding machines can be bought for about $100. The thermal binding machines sell for $500 and up.
conceptual models
Very basically: * specificity - the better 'fit' the substrate, the higher the rate of catalysis. * temperature - higher temp = more kinetic energy = faster eaction. However, too high and the enzyme becomes irreversibly denatured and will not work at all. (denatured = the folding of the peptide chains are disrupted, meaning that the shape changes and the substrates no longer fit). The temperature at which the reaction occurs at the fastest rate is called the optimum temperature. * pH - enzymes have specific pH that they work best at (the optimum/optimal pH), as pH can also affect the bonds holding the tertiary structure together (especially ionic bonds), denaturing the enzyme. * concentration of enzyme and substrate - rate of reaction is proportional to the enzyme/substrate concentration. However, at a given enzyme concentration, substrate conc is proprtional to rate up to a point when the enzyme becomes saturated and the rate remains constant. * cofactors/coenzymes - some enzymes require interaction with other molecules to show full catalytic activity. * inhibitors - the presence of an inhibitor lowers the rate of catalysis. There are competitive, uncompetitive, non-competitive and mixed inhibitors, they can bind reversibly or irreversibly, at the active site or an allosteric site... That's a very simple, school textbook answer (and I may have forgotten a factor?). For more detail, any biochemistry textbook should be able to help.
To illustrate something in larger or smaller scale so one can easily visualize the whole picture
The website Office Depot has many types of binding systems available to businessmen. They come in a variety of different models with prices ranging from $70 to $200.
The problem with our current models is that there is not enough data to allow us to determine which of the popular models are best. A model may come to be accepted if new data supports it, while at the same time contradicting other models.
Jean Pierre Kernevez has written: 'Enzyme mathematics' -- subject(s): Mathematical models, Immobilized enzymes