The responsibilities of a priest is to do human sacrifices in front of temples so everybody can see. The bishop helped the priest but wasn't as important as the priest.
Disulfide bridges can be found in tertiary and quaternary structure levels of protein organization.
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What does a disulfide bridge in a protein do and what is its function?</h3><h3>
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Disulfide bonds or S-S bonds are other names for disulfide bridges. The establishment of these covalent bonds, which are formed between the sulfur atoms of two cysteine amino acids, stabilizes the tertiary and higher-order structure of proteins.
A frequent method utilized by nature to stabilize many proteins is the formation of disulfide bridges. These disulfide linkages are frequently observed in extracellular proteins that cells produce. The endoplasmic reticulum, an organelle, is where disulfide bridges are formed in eukaryotic species. When numerous proteins enter the secretory route for folding, disulfide linkages are formed between cysteine residues.
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European imperialism was motivated by a desire for economic both regions.
Dr. Croteau explains to students in his methodology class that when they are using a mixed design, they are essentially using a(n) factorial design with multiple independent variables.
Methodology is studying the methods used in field and the theories or principles behind them, so that you can develop a approach which matches your requirements.
Mixed design is an approach in which the researcher have to examines both the potential differences between two or more separate groups of participants and also the individual changes over time.
Factorial design is necessary when interactions are there to avoid misleading conclusions. They allow the effects of a factor to be estimated at several levels of a factor, that can yield a conclusion that are valid over a range of experimental conditions.
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