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Proteins

Proteins are the macromolecules coded in our DNA that function as a biocatalyst and build our body. Apart from Biological knowledge, there are spectacular concepts in the field of proteins. How does a protein produce a function, how do they interact, how did they evolve and how do protein mutations cause disease.

500 Questions

Simple proteins are composed of only what?

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Simple proteins are composed of only amino acids. These proteins are also called monomeric proteins because they consist of a single polypeptide chain. The sequence of amino acids determines the structure and function of the protein.

Why are some proteins water soluble and others proteins are not?

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The solubility of proteins in water is determined by their structure and amino acid composition. Proteins with a high proportion of hydrophilic amino acids (such as charged and polar amino acids) tend to be water soluble. Conversely, proteins with a high proportion of hydrophobic amino acids (such as nonpolar amino acids) tend to be insoluble in water. Additionally, the presence of strong intra- or intermolecular forces (such as disulfide bonds) can also contribute to protein insolubility in water.

What are the two most important antimicrobial proteins?

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The two most important antimicrobial proteins are defensins and cathelicidins. Defensins are small cationic peptides that can bind to and disrupt the cell membranes of bacteria, fungi, and viruses. Cathelicidins are also cationic peptides that can kill microbes by disrupting their cell membranes and by modulating the immune response.

What are three types of fibrous proteins?

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The three types of fibrous proteins are collagen, keratin, and elastin. Collagen provides structure and strength to connective tissues such as tendons and skin. Keratin makes up the structure of hair, nails, and the outer layer of skin. Elastin allows tissues and organs to stretch and return to their original shape.

How do proteins know what to do?

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Proteins are produced according to the information encoded in our DNA. They have specific three-dimensional structures that enable them to interact with other molecules in a precise manner. Their functions are dictated by their structure, which allows them to recognize and bind to specific molecules, catalyze biochemical reactions, transmit signals within cells, or provide structural support, among other roles. In summary, proteins know what to do based on their intrinsic properties and the specific molecular interactions they can form.

How much fat and proteins in yoghurt?

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Yoghurt typically contains between 5% and 15% protein.

Are enzymes proteins?

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Most enzymes are proteins, yes. However, the statement (used some number of years ago) that all enzymes are proteins is false. There are a few (but important) exceptions to that generalization.

How does the sequence of DNA affect the function of a protein?

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The sequence of nucleotides in DNA molecule is equivalent and is closely related to an amino acid sequence in the protein molecule. If for any reason the sequence of DNA nucleotides changes it will be reflected in amino acid sequence in the protein. Moreover, the correct sequence of amino acid in the protein will form the correct three-dimensional structure, or tertiary structure, that will confer the biological activity to protein. If a wrong amino acid is translated from a mutated gene in the DNA could change the spatial structure of the protein and therefore modify or erase its biological function.

What are proteins carbohydrates?

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The carbohydrate contains solid elements called "Clint" and protein contains the pretty element called "Bailo".

What are proteins secondary structures?

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Unlike the primary structure, the secondary structure is defined as the local conformation of the protein's backbone. Protein secondary structures are grouped in three major types: helices (being the most common the alpha helices), pleated sheets (also called beta structures), and turns.


The combination of these three kind of secondary structures give a wide variety of forms of the protein molecules. These combinations are named supersecondary structures or motifs and occur in many unrelated globular proteins. As examples of motifs found in protein structures are: a) the beta-alpha-beta motif, the most common supersecondary structure (consists in a right-handed cross-over connection between two consecutive parallel strands of a beta sheet by an alpha helix); b) the beta hairpin motif, that consists of an antiparallel beta sheet formed by sequential segments of polypeptide chain that are connected by relatively tight reverse turns; c) the alpha-alpha motif, two successive antiparallel alpha helices pack each other with their axes inclined (one common protein with this structure is the alpha keratin); and d) the beta barrels, that are extended beta sheets that often roll up.

What atoms are found I am proteins?

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Proteins contain hydrogen, oxygen, carbon, and nitrogen atoms.

What is the major building block for proteins?

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The major and basic building blocks of proteins are the amino acids.

What makes proteins three-dimensional?

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Hydrophobic interactions cause proteins to form into a three-dimensional shape.

What are proteins that recognize specific proteins on bacteria?

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Simple the answer is an Antibody!

Does DNA synthesize proteins?

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DNA does not synthesize proteins. But they code for the message needed for the proteins. DNA transcribe mRNA first in the nucleus and send out to cytoplasm. The protein synthesis machinery in the cytoplasm (ribosome) will synthesize proteins according to the message in mRNA.

What is the main difference between protein electrophoresis and nucleic acid electrophoresis?

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There are many similarities and differences between protein and DNA electrophoresis.

Similarities:

  • PAGE protein and DNA electrophoresis both cause separation by size, creating bands that are viewed by the scientist or a machine. The smallest segments more the fastest due to less friction with the surface of their medium or equipment.
  • The movement of charges through the medium is what causes the DNA or proteins to move. Electrons move from the negative to positive end of the gel or capillary tube.

Differences:
  • In PAGE protein electrophoresis, a polyacrylamide gel is used to prevent convection from altering the movement of the proteins. If the proteins are charged, and there is a worry that the charge will affect the mobility of the protein segments, 1% SDS can be added to get rid of the mass/charge issue. This way, only the mass of the segment determines how far it moves. In DNA capillary electrophoresis, the size of the capillary is so small that it does not have room for convection to occur (it is only 20-50 microns wide). Thus, there is no medium in the capillary but DNA itself.
  • In protein electrophoresis, the proteins are often dyed so their movement can be viewed with the naked eye, or a machine. With DNA capillary electrophoresis, DNA strands are made through DNA replication with dNTPs that are fluorescently labeled for the different nucleotides. Each base is labeled a different color. A fine laser lights up the DNA strand in the capillary tube and reads what color fluoresces. This is how the nucleotide is identified.
  • Protein PAGE electrophoresis is used to determine the purity of a protein sample. It can also be used to see how large the chains are that make up a multi-chain protein if a denaturing agent is added. DNA electrophoresis is used to get the order of nucleotides in a DNA sequence. It is done by chopping the DNA sequence into many smaller bits and sequencing them, then putting them back together by lining them up according to sequence overlaps. This is called the "shotgun" method. Protein electrophoresis can figure out the order of about 15-20 amino acids by a similar method, but DNA electrophoresis can get up to 1000 nucleotides (~300 amino acids). DNA electrophoresis is limited by the low probability that the DNA sequence would be cut into a segment greater than 1000 nucleotides.

Are microtubules tubelike proteins?

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Microtubules and microfilaments are cellular cytoskeletal networks. Microtubules are tubular proteins made by tubulin polymers. they have role in cell structure, cell movement, mitosis, gene regulation and so on.

Is the nucleus the site of protein assembly?

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No. The protein assembly, or protein synthesis, is taking place in the cytosol, particularly in the ribosomes.

Where would you find hydrogen bonds proteins?

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The most common bond in hydrogen is a compound one.

What proteins are found in chromatin?

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You may be looking for the term "histones," which are the protein component of chromatin (which comprises chromosomes).
Histones are proteins around which DNA winds, making it dense and compact; this results in the denser form of chromatin, known as "heterochromatin." Histones thus play a role in regulating the expression of genes (because they cannot be expressed whilst compacted). When histones are modified, they can change shape or charge and release the tightly-wound DNA so that the genes can be expressed; this looser form of chromatin is known as "euchromatin."
Together, heterochromatin and euchromatin make up chromosomes.

http://en.wikipedia.org/wiki/Histone

Who modifies and packages new synthesized proteins?

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The Golgi Apparatus modifies and packages newly synthesized proteins sent from the Rough Endoplasmic Reticulum.

Does plasma contain proteins?

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Yes. The major proteins found in plasma are fibrinogen, the protein that helps the blood to clot, antibodies, and enzymes.

What is the Folding of proteins?

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Protein folding determines the shape of the protein, and thus what it does, because it is the shape of the protein which enables it to perform its function. For example, enzymes need to have exactly the right shape to fit with the molecules they are working with to catalyze them. Also, hemoglobin is specifically folded with four pocket like areas to allow oxygen to attach to it. The shape of the protein is specific to the function that it is performing, and is different for each protein. If there is even a slight change in the make up of the protein, or a mutation (the amino acids are messed up) then the protein will fold differently. Even a slight change in the composition of the protein can disable the protein from properly performing the function which it is meant to do.