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svet-max [94.6K]
3 years ago
14

In the past 20 years, the development of NMR technology has expanded its application in the field of drugs from identification o

f chemical structures of drugs in vitro to analysis of drugs and their metabolites in body fluids and tissues. Compared with other analytical methods, what are the characteristics of NM R method?
Biology
1 answer:
Virty [35]3 years ago
3 0

Answer:

(1) the simplicity does not require complicated extraction or derivatization of the sample, thus reducing the error caused by the extraction;

(2) Non-invasive: After NMR analysis, biological samples with limited sampling volume can also be used for other treatments, and even non-invasive analysis can be carried out on the whole organism;

(3) Continuous NMR can dynamically monitor the whole biological system without disturbing all kinds of balances in the biological body and realize in-vivo analysis of drugs;

(4) The high resolution N MR spectral line is of the order of Hz, which can provide structural information at molecular level;

(5) Multi-objective can detect drugs and their metabolites under the same physical condition without groping for analysis conditions.

Explanation:

http://www.creative-biostructure.com/nmr-services_28.htm

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allsm [11]

Answer:

Protein B has a higher affinity for ligand C than protein A

Explanation:

Binding affinity is a measure of the strength of the bonds or interactions between a single biomolecule or receptor to its ligand. A ligand is usually a small molecule that binds to a specific receptor.

The receptor is usually a large molecule that contains a specific site for the binding of ligand.

Binding affinity is usually measured by the equilibrium dissociation constant (KD). The equilibrium dissociation constant KD is a ratio of the dissociation and the association of ligand to the receptor. The value of KD is used to evaluate and compare the strengths of bimolecular interactions.  The larger the KD value, the more weakly the target molecule and ligand are attracted to and bind to one another.

The higher the dissociation constant (KD), the weaker the affinity is between the interacting molecules, whereas, the smaller the KD value, the greater the binding affinity of the ligand for its target.

Protein B has a KD value of 10⁻⁹ M while Protein A has a KD of 10⁻⁶ M.

Ration of KD of protein B to protein A = 10⁻⁹ M/10⁻⁶ M = 10⁻³

Therefore, protein B has a KD value which is 1000 times smaller than the KD of protein A.

8 0
3 years ago
True or false: during stressful events, there is decreased blood supply to the skin, which results in "goose bumps."
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False.
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nalin [4]
It starts with a seed, than when the seed is on the ground it germinates.
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Answer:

i believe that the awnser is A

Explanation:

6 0
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4 0
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