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True or False 'A change in the primary sequence of a protein can affect allosteric regulation'?
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∙ 15y ago
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What is the level of protein structure is the amino acid sequence of the protein?
Quaternary tertiary secondary primary is the sequence.
The sequence of amino acids joined together refers to the?
Peptide sequence or amino acid sequence is the order in which amino acid residues, connected by peptide bonds, lie in the chain in peptides and proteins. The sequence is generally reported from the N-terminal end containing free amino group to the C-terminal end containing free carboxyl group. Peptide sequence is often called protein sequence if it represents the primary structure of a protein.
What determines protein structure?
The primary structure of proteins is the sequence of amino acids. The sequence is determined by DNA and genetics. RNA copies the code from DNA and it takes it over to the ribosomes. Then the amino acids are sequenced based on the "instructions."
What is non allosteric enzymes?
A second and reversible form of regulation is known as allosteric regulation In allosteric regulation, regulatory molecules bind reversibly to the protein, altering its confirmation, which in turn alters its activity. Such allosteric effectors are not covalently attached to the protein. Here, the activity of a protein is positively regulated by the binding of a factor. This factor could be a small molecule or another protein. What is important is that the allosteric binding site is distinct from the enzyme's catalytic site. That is what allosteric means, other site. An allosteric effector can also act negatively, inhibiting enzyme activity. Because allosteric regulators do not bind to the same site on the protein as the substrate, changing substrate concentration generally does not alter their effects. Of course there are other types of regulation as well. Active site inhibitors: An inhibitory factor may bind to and block the active site. If this binding is reversible, then increasing the amount of substrate can over-come the inhibition. An inhibitor of this type is known as a competitive inhibitor. In some cases, the inhibitor chemically reacts with the enzyme, forming a covalent bond. Because this type of inhibitor is essentially irreversible, increasing substrate concentration can not overcome inhibition. These are therefore known as a noncompetitive inhibitors. Biofundamentals - Regulating protein activity 9/27/08 11:13 AM file:///Users/klymkowsky/Documents/WebSites/virtual/Biofundamentals/lectureNotes/Topic3-6_Protein%20Activity.htm Page 3 of 6 Allosteric effectors are also non-competitive, since they do not compete with substrate for binding to the active site. A protein binds an allosteric regulator - what happens to the protein? Why are allosteric regulators not "competitive"? What makes an inhibitor that binds to the active site of an enzyme "non-competitive" ? Post-translational regulation: Proteins may be modified after synthesis - this process is known as post-translational modification. A number of posttranslational modifications have been found to occur within cells. The first type involve the covalent addition of specific groups to the protein - these groups can range from phosphate groups (phosphorylation), an acetate group (acetylation), the attachment of lipid/hydrophobic groups (lipid modification), or carbohydrates (glycosylation) . Often post-translational modifications are reversible, one enzyme adds the modifying group, and another can act to remove it. For example, proteins are phosphorylated by enzymes known as protein kinases, while protein phosphatases remove phosphate groups. Post-translational modifications act in much the same way as do allosteric effectors, they modify the activity of the polypeptide to which they are attached. They can also modify a proteins interactions with other proteins, the protein's localization within the cell, or its stability. Proteolytic processing: Another method for regulating protein activity involves the cleavage of the polypeptide chain. Many proteins are originally synthesized in a longer, and inactive "pro-form". To become active the propeptide must be removed - it is cut by a protease. This proteolytic processing activates the protein. Proteolytic processing is itself often regulated. A protein is normally found free in the cytoplasm; where would you expect it would be found following addition of a lipid group? What are the advantages/disadvantages of using proteolytic activation, compared to allosteric activation of a protein? Biofundamentals - Regulating protein activity 9/27/08 11:13 AM file:///Users/klymkowsky/Documents/WebSites/virtual/Biofundamentals/lectureNotes/Topic3-6_Protein%20Activity.htm Page 4 of 6 activation, compared to allosteric activation of a protein? Why are enzymes required for post-translational modification? Do you think post-translational modification requires energy? Telling proteins where to go: Translation of proteins occurs in the cytoplasm, where mature ribosomes are located. If no information is added, a newly synthesized polypeptide will remain in the cytoplasm, that is its default location. Yet even in the structurally simplest of cells, the prokaryotes (bacteria and archaea), there is more than one place that a protein may end up: it can remain in the cytoplasm, it can be inserted in the plasma membrane or it may be secreted from the cell. Both membrane and secreted polypeptides must be inserted into, or pass through, the plasma membrane. Polypeptides destined for the membrane or for secretion are generally marked by a specific tag, known as a signal sequence. The signal sequence consists of a stretch of hydrophobic amino acids, often at the N-terminus of the polypeptide. As the signal sequence emerges from the ribosome it interacts with a signal recognition particle or SRP - a complex of polypeptides and a structural RNA. The binding of SRP to the signal sequence causes translation to pause. The mRNA/ribosome/nascent polypeptide/SRP complex will find (by diffusion), and attach to, a ribosome/SRP receptor complex on the cytoplasmic surface of the plasma membrane. This ribosome/SRP receptor is associated with a polypeptide pore. When the ribosome/SRP complex docks with the receptor, translation resumes and the nascent polypeptide passes through a protein pore and so through the membrane. As the polypeptide emerges on the extracytoplasmic side of the membrane, the signal sequence is generally removed by an enzyme, signal sequence peptidase. If the polypeptide is a membrane protein, it will remain within the membrane. If it is a secreted polypeptide, it will be released into the periplasmic space. _armanfiroz_
The sequence of amino acids that makes up a protein molecule is determined by the sequence of?
The primary structure of a protein is the sequence of amino acids in the protein. This is determined by the sequence of bases in the DNA ie by the genetic code. Each group of three bases in DNA codes for one amino acid in the protein ie it is a triplet code.
What is the level of protein structure is the amino acid sequence of the protein?
Quaternary tertiary secondary primary is the sequence.
What is primary structure of a protein and what causes it?
Primary structure of the protein is simply its amino acid sequence. It is the sequence in which amino acids are added during protein synthesis.
Distinguish between allosteric activation and cooperativity?
cooperativity is an interaction of the subunits of a protein whereby a conformational change in one subunit is transmitted to all others. allosteric regulation is when an activation molecule bonds to an active site where the subunits join.
What is the primairy structure of a protein?
Primary - the sequence of amino acids that make up a protein
The sequence of amino acids joined together refers to the?
Peptide sequence or amino acid sequence is the order in which amino acid residues, connected by peptide bonds, lie in the chain in peptides and proteins. The sequence is generally reported from the N-terminal end containing free amino group to the C-terminal end containing free carboxyl group. Peptide sequence is often called protein sequence if it represents the primary structure of a protein.
What is the Primary level of a protein structure?
Is the sequence of amino acids that form the protein
The primary structure of a protein refers to?
The number and sequence of amino acids
Difference between primary and secondary sequence database?
Primary sequence databases store experimentally determined sequences, while secondary databases compile and organize information from primary databases along with additional annotations, classifications, and analyses. Primary databases provide raw sequence data, while secondary databases offer curated and annotated information to facilitate research and analysis.
What is non allosteric enzymes?
A second and reversible form of regulation is known as allosteric regulation In allosteric regulation, regulatory molecules bind reversibly to the protein, altering its confirmation, which in turn alters its activity. Such allosteric effectors are not covalently attached to the protein. Here, the activity of a protein is positively regulated by the binding of a factor. This factor could be a small molecule or another protein. What is important is that the allosteric binding site is distinct from the enzyme's catalytic site. That is what allosteric means, other site. An allosteric effector can also act negatively, inhibiting enzyme activity. Because allosteric regulators do not bind to the same site on the protein as the substrate, changing substrate concentration generally does not alter their effects. Of course there are other types of regulation as well. Active site inhibitors: An inhibitory factor may bind to and block the active site. If this binding is reversible, then increasing the amount of substrate can over-come the inhibition. An inhibitor of this type is known as a competitive inhibitor. In some cases, the inhibitor chemically reacts with the enzyme, forming a covalent bond. Because this type of inhibitor is essentially irreversible, increasing substrate concentration can not overcome inhibition. These are therefore known as a noncompetitive inhibitors. Biofundamentals - Regulating protein activity 9/27/08 11:13 AM file:///Users/klymkowsky/Documents/WebSites/virtual/Biofundamentals/lectureNotes/Topic3-6_Protein%20Activity.htm Page 3 of 6 Allosteric effectors are also non-competitive, since they do not compete with substrate for binding to the active site. A protein binds an allosteric regulator - what happens to the protein? Why are allosteric regulators not "competitive"? What makes an inhibitor that binds to the active site of an enzyme "non-competitive" ? Post-translational regulation: Proteins may be modified after synthesis - this process is known as post-translational modification. A number of posttranslational modifications have been found to occur within cells. The first type involve the covalent addition of specific groups to the protein - these groups can range from phosphate groups (phosphorylation), an acetate group (acetylation), the attachment of lipid/hydrophobic groups (lipid modification), or carbohydrates (glycosylation) . Often post-translational modifications are reversible, one enzyme adds the modifying group, and another can act to remove it. For example, proteins are phosphorylated by enzymes known as protein kinases, while protein phosphatases remove phosphate groups. Post-translational modifications act in much the same way as do allosteric effectors, they modify the activity of the polypeptide to which they are attached. They can also modify a proteins interactions with other proteins, the protein's localization within the cell, or its stability. Proteolytic processing: Another method for regulating protein activity involves the cleavage of the polypeptide chain. Many proteins are originally synthesized in a longer, and inactive "pro-form". To become active the propeptide must be removed - it is cut by a protease. This proteolytic processing activates the protein. Proteolytic processing is itself often regulated. A protein is normally found free in the cytoplasm; where would you expect it would be found following addition of a lipid group? What are the advantages/disadvantages of using proteolytic activation, compared to allosteric activation of a protein? Biofundamentals - Regulating protein activity 9/27/08 11:13 AM file:///Users/klymkowsky/Documents/WebSites/virtual/Biofundamentals/lectureNotes/Topic3-6_Protein%20Activity.htm Page 4 of 6 activation, compared to allosteric activation of a protein? Why are enzymes required for post-translational modification? Do you think post-translational modification requires energy? Telling proteins where to go: Translation of proteins occurs in the cytoplasm, where mature ribosomes are located. If no information is added, a newly synthesized polypeptide will remain in the cytoplasm, that is its default location. Yet even in the structurally simplest of cells, the prokaryotes (bacteria and archaea), there is more than one place that a protein may end up: it can remain in the cytoplasm, it can be inserted in the plasma membrane or it may be secreted from the cell. Both membrane and secreted polypeptides must be inserted into, or pass through, the plasma membrane. Polypeptides destined for the membrane or for secretion are generally marked by a specific tag, known as a signal sequence. The signal sequence consists of a stretch of hydrophobic amino acids, often at the N-terminus of the polypeptide. As the signal sequence emerges from the ribosome it interacts with a signal recognition particle or SRP - a complex of polypeptides and a structural RNA. The binding of SRP to the signal sequence causes translation to pause. The mRNA/ribosome/nascent polypeptide/SRP complex will find (by diffusion), and attach to, a ribosome/SRP receptor complex on the cytoplasmic surface of the plasma membrane. This ribosome/SRP receptor is associated with a polypeptide pore. When the ribosome/SRP complex docks with the receptor, translation resumes and the nascent polypeptide passes through a protein pore and so through the membrane. As the polypeptide emerges on the extracytoplasmic side of the membrane, the signal sequence is generally removed by an enzyme, signal sequence peptidase. If the polypeptide is a membrane protein, it will remain within the membrane. If it is a secreted polypeptide, it will be released into the periplasmic space. _armanfiroz_
What determines protein structure?
The primary structure of proteins is the sequence of amino acids. The sequence is determined by DNA and genetics. RNA copies the code from DNA and it takes it over to the ribosomes. Then the amino acids are sequenced based on the "instructions."
The primary structure of a protein is determined by the sequence of what?
Amino acids, the building blocks of proteins.
The sequence of amino acids that makes up a protein molecule is determined by the sequence of?
The primary structure of a protein is the sequence of amino acids in the protein. This is determined by the sequence of bases in the DNA ie by the genetic code. Each group of three bases in DNA codes for one amino acid in the protein ie it is a triplet code.
