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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    The effects of temperature on enzyme activity. Top: increasing temperature increases the rate of reaction (Q10 coefficient). Middle: the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom: consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.

  3. Q10 (temperature coefficient) - Wikipedia

    en.wikipedia.org/wiki/Q10_(temperature_coefficient)

    The effects of temperature on enzyme activity. Top - increasing temperature increases the rate of reaction (Q 10 coefficient). Middle - the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom - consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    An enzyme's activity decreases markedly outside its optimal temperature and pH, and many enzymes are (permanently) denatured when exposed to excessive heat, losing their structure and catalytic properties.

  5. Carbaminohemoglobin - Wikipedia

    en.wikipedia.org/wiki/Carbaminohemoglobin

    Temperature: A factor such as temperature can affect the binding and release of gases by hemoglobin. The effect of temperature on the binding of carbon dioxide to hemoglobin is less noticeable compared to other gases, but this factor can still have an influence on the overall regulation of gas exchange.

  6. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...

  7. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Protein backbones are very stable in water at neutral pH and room temperature, although the rate of hydrolysis of different peptide bonds can vary. The half life of a peptide bond under normal conditions can range from 7 years to 350 years, even higher for peptides protected by modified terminus or within the protein interior.

  8. Basal metabolic rate - Wikipedia

    en.wikipedia.org/wiki/Basal_metabolic_rate

    For example under calorie restriction whole body metabolic rate goes down with increasing levels of restriction, but body temperature also follows the same pattern. By manipulating the ambient temperature and exposure to wind it was shown in mice and hamsters that body temperature is a more important modulator of lifespan than metabolic rate. [45]

  9. Isoleucine - Wikipedia

    en.wikipedia.org/wiki/Isoleucine

    Isoleucine (symbol Ile or I) [1] is an α-amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated −NH + 3 form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a hydrocarbon side chain with a branch (a central carbon atom bound to three other ...