ssb protein bind to the lagging strand as leading strand is invovled in dna replication and lagging strand is invovled in okazaki fragment formation
Due to change in nucleotide, a completely different protein is coded for. The normal protein has glutamic acid, is hydrophillic; however, the mutated protein incorporates valine, a hydrophobic amino acid instead. This causes the overall haemoglobin protein to distort into a sickle shape, rather than a concave shape. As a result, sickle cells have a much shorter lifespan than their normal counterparts.
Ribosomes would be the simple answer, but they only bind to the endoplasmic reticulum once it begins to synthesize a protein. Other bumpy structures you may encounter on the endoplasmic reticulum are proteins and vesicles.
= Protein Synthesis = ----Legend:Process whereby DNA encodes for the production of amino acids and proteins. This process can be divided into two parts:1. TranscriptionBefore the synthesis of a protein begins, the corresponding RNA molecule is produced by RNA transcription. One strand of the DNA double helix is used as a template by the RNA polymerase to synthesize a messenger RNA (mRNA). This mRNA migrates from the nucleus to the cytoplasm. During this step, mRNA goes through different types of maturation including one called splicingwhen the non-coding sequences are eliminated. The coding mRNA sequence can be described as a unit of three nucleotides called a codon. 2. TranslationThe ribosome binds to the mRNA at the start codon (AUG) that is recognized only by the initiator tRNA. The ribosome proceeds to the elongation phase of protein synthesis. During this stage, complexes, composed of an amino acid linked to tRNA, sequentially bind to the appropriate codon in mRNA by forming complementary base pairs with the tRNA anticodon. The ribosome moves from codon to codon along the mRNA. Amino acids are added one by one, translated into polypeptidic sequences dictated by DNA and represented by mRNA. At the end, a release factor binds to the stop codon, terminating translation and releasing the complete polypeptide from the ribosome. One specific amino acid can correspond to more than one codon. The genetic code is said to be degenerate.
Since squids do not have haemoglobin they use haemocyanin to bind and transport oxygen throughout their body.
Hemoglobin is a protein in red blood cells that carries oxygen from the lungs to the rest of the body and transports carbon dioxide back to the lungs to be exhaled. In animals, hemoglobin is crucial for the respiratory system to function properly and maintain homeostasis by ensuring proper oxygen delivery. The structure of hemoglobin allows it to bind to oxygen in the lungs and release it in tissues where it is needed for energy production.
Triphosphate deoxyribonucleotides form hydrogen bonds with their complements in a DNA parent strand during transcription of the leading strand of DNA. Example Adenine nucleotides bind to thymine nucleotides Guanine nucleotides bind to Cytosine nucleotides
The 5 prime end of the strand.
DNA ligase is the enzyme that binds together the Okazaki fragments on the lagging strand during DNA replication. It forms phosphodiester bonds between adjacent nucleotides to create a continuous strand of DNA.
The molecule that can bind to a receptor protein is called a ligand.
The two strands of a DNA molecule are antiparallel to one another (the backbone of one strand runs from 5'-3' while the complimentary strand runs 3'-5'). Unfortunately, DNA polymerase, the enzyme responsible for replicating DNA, can only make DNA in a 5'-3' direction (and read DNA in the 3'-5' direction). Also, it needs a "primer" to give it a place to bind and start replication. So this creates a problem when synthesizing the 3'-5' stand because your enzyme will only synthesize 5'-3'. During replication this is solved by synthesizing small pieces of DNA ahead of the replication fork on the 5'-3' mother strand. Thus we have one daughter strand which is synthesized as a continuous piece of DNA (called the leading strand) and one daughter strand which is synthesized in small, discontinuous pieces (called the lagging strand). However, at the extreme end of the DNA, we run into another problem. The leading stand can be made to the very end, but the lagging strand cannot because you need the RNA primer upstream to begin each piece of the lagging strand DNA but at the end of the DNA there is nothing for this piece to attach to. Thus, the last section of the lagging strand cannot be synthesized and after several rounds of DNA replication, the DNA molecule gets smaller and smaller. This is "the end of replication problem" and it is solved by putting a DNA cap on the ends of DNA called a telomere which does not code for any protein, thus when this information is lost it does not have severe consequences for the cell.
role of ssb protein in dna replication is when the double stranded dna is brought in the single stranded form during replication the ssb bind to the single stranded dna so that the ss dna remain in the the single stranded form and when replication process is completed these protein get dissociated from the dna
DNA is made of of two complimentary strands, the coding strand and the template strand. When DNA is transcribed (made into messenger RNA which can be converted by ribosomes into proteins) the DNA splits open and free nucleotide bases bind to the template strand. DNA is made of T/C/G/A and RNA is made of U/C/G/A nucleotide bases. G and C bind (they are said to be 'complimentary') A and T bind and in RNA U and A bind (so U replaces T.) The newly formed RNA strand (made on the template stand of DNA) is 'complimentary' to the template but the same as the coding strand of DNA. Hence the template is used to produce RNA which is a copy of the coding strand. Either strand of DNA can act as the template/coding strand. Hope that is a little bit helpful!
Protein A and protein G differ in their ability to bind to specific antibodies based on their binding preferences. Protein A primarily binds to antibodies from the IgG class, while protein G has a broader binding range and can bind to antibodies from multiple classes, including IgG, IgM, and IgA.
If a membrane protein were unable to bind to a signaling molecule, it would lead to a disruption in cell signaling pathways. This could result in altered cellular responses, such as improper communication between cells or impaired signaling cascades, leading to dysfunctional physiological processes.
Enhancers do not directly bind to repressor proteins. Enhancers typically bind to activator proteins, which in turn help recruit RNA polymerase to the promoter region of a gene, leading to gene transcription. Repressor proteins, on the other hand, bind to specific DNA sequences to inhibit gene transcription.
Your question is ambiguous and could refer to any of the following:Prokaryotes employ proteins that recognise termination sites, including the 'tus' protein. These bind and act as one way gates, so that termination occurs in a predefined location. The exact mechanism of termination is unknown, but is presumed to be a simple meeting of two replication forks causing the apparatus to stop and dissociate. Replication is successful without the tus protein.In eukaryotes, termination of replication is poorly understood.Eukaryotes have linear DNA, and as such cannot replicate a short region on the end of each DNA molecule on the lagging strand, since replication requires RNA primers, and there will be nowhere for the primer to bind (it is later degraded so cannot be kept). Eukaryotes therefore use telomeress, which are GT rich repeating units that 'protect' the end of the DNA and can be placed without the use of a templace (the telomerase enzyme itself has an RNA template within it). The sequence of the telomere is species dependent. There will always be an overhang on the telomere, where telomerase added bases that could not be replicated on the other strand (as there is still nowhere to put the primer).
Calcium ions need to bind to the protein troponin in order to initiate muscle contraction.