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Since A Lens Is Made Of Protein What Effect Might The Preserving Fluid Used In Lab Have On The Structure Of The Lens And How Would This Affect The Clarity?
The preserving fluid in the lab may cause the protein structure of the lens to denature, altering its shape and affecting its clarity. Denaturation can lead to cloudiness or opacity in the lens, reducing its ability to refract light properly for clear vision.
Why is X-ray radiation required in protein structure determination?
Protein structure determination is basically crystallography i.e. finding out the arrangements of atoms. This technique uses Diffraction maxima and minima to determine 3D structures. For diffraction to occur, the size of the obstacle must be close to the wavelength of light used. Since the obstacles in this case are molecules, we use X rays, whose wavelength is comparable to radius of molecules.
How many grams of nitrogen are contained in 2500 kcal diet that provides 15 percent of the energy as protein?
To calculate the amount of nitrogen in a diet, you typically assume that 16% of protein is nitrogen. In this case, if 15% of the energy in the diet comes from protein, you can calculate the total protein in the diet (2500 kcal * 0.15 = 375 kcal from protein). Then, convert this to grams of protein using the fact that protein provides 4 kcal/g. Finally, since protein is about 16% nitrogen, you can calculate the total grams of nitrogen in the diet.
How many resonance structure for BeF2?
There is only one resonance structure for BeF2 since beryllium (Be) does not form multiple bonds due to its electron configuration (2 valence electrons). Therefore, the Lewis structure of BeF2 shows two single bonds between beryllium and each fluorine atom.
Who discover photo electric effect and what date?
The photo electric effect was explained by Einstein in 1905 when he theorized that light could transfer its energy like a particle and knock electrons out of metals. But the actual effect had been observed by a number of scientists since 1887, they just couldn't come up with a satisfactory theory that explained everything they observed. I believe he got the Nobel Prize for his photo electric effect theory, although he is more famous for his Relativity theories.
Since A Lens Is Made Of Protein What Effect Might The Preserving Fluid Used In Lab Have On The Structure Of The Lens And How Would This Affect The Clarity?
The preserving fluid in the lab may cause the protein structure of the lens to denature, altering its shape and affecting its clarity. Denaturation can lead to cloudiness or opacity in the lens, reducing its ability to refract light properly for clear vision.
What is a tertiary protein structure exemplified by?
A tertiary protein structure is the three-dimensional arrangement of a polypeptide chain. An example of a tertiary protein structure is the globular shape of enzymes like catalase or lysozyme. This structure is crucial for the protein's function as it determines the active sites and binding sites.
How is Protein Structure related to its function?
Protein structure is directly related to its function because the three-dimensional shape of a protein determines its ability to interact with other molecules. This shape allows the protein to perform specific functions, such as enzymatic reactions, signal transduction, or structural support. Any changes in the protein structure can alter its function and potentially lead to dysfunction or disease.
Are foods more filling if they are high in fiber or high in protein?
Fiber has the bulk to physically fill the stomach giving a full feeling. Protein provides a longer-lasting effect of satiation since it is used more slowly.
How does protein denatured?
It breaks the hydrogen bonds and hydrophobic interactions between different parts of the protein molecule. Proteins are composed of amino acid subunits linked together by peptide bonds—this is called a polypeptide and is also known as the primary structure of a protein. The primary structure interacts with itself (also known as folding) forming hydrogen bonds and hydrophobic interactions with different parts of the same molecule. Heat disrupts the hydrogen bonds and hydrophobic interactions leaving the protein to unfold when it is heated. Since heat is not strong enough to break the peptide bonds between the amino acid subunits, the primary structure remains intact. Once the protein is cooled again, the hydrogen bonds and hydrophobic interactions can reform since they are based on the makeup of the primary structure and it hasn't changed. :) Hope this helps.
Which methods you can use to determine the primary structure of an enzyme?
Off the top of my head: techniques such as chemical and enzymatic degredation (particularly if they are targeted) coupled with various analytical techniques particularly mass spectrometry and NMR. X-ray crystallography could also be used if the enzyme can be crystallised.
Hemoglobin represents which level of protein organization?
Haemoglobin has a protein structure upto quarternary structure since it is a dimer made up of two monomeric units, each of which are two in number. Thus the overall structure has 4 monomeric units.
What are the example of structural protein?
Hemoglobin - formed with alpha helices and/or beta sheets, but as one, contiguous polypeptide. Superoxide dismutase would be a good example of a quaternary structure protein, since it is made of more than one polypeptide chain.
How does heat denatured protein?
It breaks the hydrogen bonds and hydrophobic interactions between different parts of the protein molecule. Proteins are composed of amino acid subunits linked together by peptide bonds—this is called a polypeptide and is also known as the primary structure of a protein. The primary structure interacts with itself (also known as folding) forming hydrogen bonds and hydrophobic interactions with different parts of the same molecule. Heat disrupts the hydrogen bonds and hydrophobic interactions leaving the protein to unfold when it is heated. Since heat is not strong enough to break the peptide bonds between the amino acid subunits, the primary structure remains intact. Once the protein is cooled again, the hydrogen bonds and hydrophobic interactions can reform since they are based on the makeup of the primary structure and it hasn't changed. :) Hope this helps.
Why is X-ray radiation required in protein structure determination?
Protein structure determination is basically crystallography i.e. finding out the arrangements of atoms. This technique uses Diffraction maxima and minima to determine 3D structures. For diffraction to occur, the size of the obstacle must be close to the wavelength of light used. Since the obstacles in this case are molecules, we use X rays, whose wavelength is comparable to radius of molecules.
What happens to the shape and function of a protein if one of the amino acids is replaced with a different type of amino acid?
It depends on the role of the amino acid that is altered. One amino acid might be replaced with no measurable effect on the protein's function; replacing another might cause a total loss of function.
Chemical denaturation of protein?
Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape.Denaturation occurs because the bonding interactions responsible for the secondary structure (hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure there are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions. which may be disrupted. Therefore, a variety of reagents and conditions can cause denaturation. The most common observation in the denaturation process is the precipitation or coagulation of the protein.
