Slide 1
... amino acid side chains to project radially. When several parallel α-helices are closely packed, their side chains may intermesh as shown, or steric constraints may cause the formation of interchain channels. The outwardly directed residues must be predominantly hydrophobic to interact with the fatty ...
... amino acid side chains to project radially. When several parallel α-helices are closely packed, their side chains may intermesh as shown, or steric constraints may cause the formation of interchain channels. The outwardly directed residues must be predominantly hydrophobic to interact with the fatty ...
13.1 RNA
... Messenger RNA An mRNA molecule is a copy of the portion of DNA that will be used to make a protein. After being made in the nucleus, mRNA travels to the cytoplasm, the site of protein synthesis. ...
... Messenger RNA An mRNA molecule is a copy of the portion of DNA that will be used to make a protein. After being made in the nucleus, mRNA travels to the cytoplasm, the site of protein synthesis. ...
Amino Acids and Proteins
... protein. The structural formulas of di- and tripeptides are written. The secondary forms of protein structure include the alpha helix, pleated sheet and collagen. The interaction of side groups to form the cross-links of tertiary structure is discussed. The breakdown in the secondary and tertiary st ...
... protein. The structural formulas of di- and tripeptides are written. The secondary forms of protein structure include the alpha helix, pleated sheet and collagen. The interaction of side groups to form the cross-links of tertiary structure is discussed. The breakdown in the secondary and tertiary st ...
Pinar Tulay cell molecules_17
... chains of amino acids, such as a dipeptide (two amino acids), a tripeptide (three), and a tetrapeptide (four). • A protein is composed of one or more long chains, or polypeptides, composed of amino acids linked by covalent bonds. ...
... chains of amino acids, such as a dipeptide (two amino acids), a tripeptide (three), and a tetrapeptide (four). • A protein is composed of one or more long chains, or polypeptides, composed of amino acids linked by covalent bonds. ...
Lecture 15: Processing of viral pre-mRNA
... • Note: many viruses have dispensed with polyA tails altogether. Rather, they trick polyA-binding protein to interact with complex 3’ mRNA structures. ...
... • Note: many viruses have dispensed with polyA tails altogether. Rather, they trick polyA-binding protein to interact with complex 3’ mRNA structures. ...
Transcript Maps
... • transcription factor (TF) General term for any protein, other than RNA polymerase, required to initiate or regulate transcription in eukaryotic cells. General factors, required for transcription of all genes, participate in formation of the transcription-initiation complex near the start site. Spe ...
... • transcription factor (TF) General term for any protein, other than RNA polymerase, required to initiate or regulate transcription in eukaryotic cells. General factors, required for transcription of all genes, participate in formation of the transcription-initiation complex near the start site. Spe ...
Novel eukaryotic enzymes modifying cell
... (gi: 119597197; region 207-428). In addition to recovering Cas1p orthologs, the search also detected numerous other eukaryotic proteins with significant expect (e)values in course of successive iterations. For example, the search recovered the Homo sapiens C7orf58 protein (gi: 119603958; e = 8xe-06) ...
... (gi: 119597197; region 207-428). In addition to recovering Cas1p orthologs, the search also detected numerous other eukaryotic proteins with significant expect (e)values in course of successive iterations. For example, the search recovered the Homo sapiens C7orf58 protein (gi: 119603958; e = 8xe-06) ...
PROTEINS Proteins are unbranched polymers of amino acids linked
... These are plant proteins, insoluble in water or neutral salt solutions, but soluble in dilute acids or alkalies. They are rich in glutamic acid. They are large molecules and can be coagulated by heat. Examples: Oryzenin of rice and glutelin of wheat. 7. Scleroproteins or Albuminoids These are fibrou ...
... These are plant proteins, insoluble in water or neutral salt solutions, but soluble in dilute acids or alkalies. They are rich in glutamic acid. They are large molecules and can be coagulated by heat. Examples: Oryzenin of rice and glutelin of wheat. 7. Scleroproteins or Albuminoids These are fibrou ...
E. coli
... During transcription, the 5' end of the RNA becomes available for ribosomal binding and undergoes translation while its 3' end is still being transcribed. This early binding of ribosomes to the RNA maintains transcript stability and promotes efficient translation. This bacterial translation system g ...
... During transcription, the 5' end of the RNA becomes available for ribosomal binding and undergoes translation while its 3' end is still being transcribed. This early binding of ribosomes to the RNA maintains transcript stability and promotes efficient translation. This bacterial translation system g ...
BCL-2 Family Proteins: Critical Checkpoints of Apoptotic
... 2) apoptotic protease : APAF-1, caspase-9, cythchrome c, mitochondrial electron transport chain 3) release during apoptosis ...
... 2) apoptotic protease : APAF-1, caspase-9, cythchrome c, mitochondrial electron transport chain 3) release during apoptosis ...
Genetic Coding in Ce..
... This is called messenger RNA (mRNA) because it acts as a messenger between DNA and the ribosomes where protein synthesis is carried out. ...
... This is called messenger RNA (mRNA) because it acts as a messenger between DNA and the ribosomes where protein synthesis is carried out. ...
Genome sequence and gene compaction of the eukaryote parasite
... The chromosome sequences were determined through a plasmid library (,3 kb inserts) and a miniBAC library (,20±25 kb inserts) totalling 15 genome equivalents (,46 Mb). All chromosomes possess a `unique sequences' core region ¯anked by two 28-kb divergently oriented regions, each including one ribosom ...
... The chromosome sequences were determined through a plasmid library (,3 kb inserts) and a miniBAC library (,20±25 kb inserts) totalling 15 genome equivalents (,46 Mb). All chromosomes possess a `unique sequences' core region ¯anked by two 28-kb divergently oriented regions, each including one ribosom ...
On the Importance of Amino Acid Sequence and Spatial Proximity of
... fit this to simple sigmoids. The fits show no clear residue dependence at the range of interaction distances typically known to be relevant to protein structure and folding (0–10 Å). This is not surprising since the fits are dominated by the data at long distances and would look very similar for scr ...
... fit this to simple sigmoids. The fits show no clear residue dependence at the range of interaction distances typically known to be relevant to protein structure and folding (0–10 Å). This is not surprising since the fits are dominated by the data at long distances and would look very similar for scr ...
emboj2009380-sup
... amplify the 342 bp Hbα p12; while the forward primer: 5’ ACGCGTCGAC (SalI)TCCACCCCTGATGCTGTTA 3’ and reverse primer: 5’ CCGCTCGAG (XhoI)GTGATACTTGTGGGCCAGG 3’ were used to amplify the 297 bp Hbβ p10. The cloning map is shown in Supplementary Figure S9C. The recombinant expression constructs were ve ...
... amplify the 342 bp Hbα p12; while the forward primer: 5’ ACGCGTCGAC (SalI)TCCACCCCTGATGCTGTTA 3’ and reverse primer: 5’ CCGCTCGAG (XhoI)GTGATACTTGTGGGCCAGG 3’ were used to amplify the 297 bp Hbβ p10. The cloning map is shown in Supplementary Figure S9C. The recombinant expression constructs were ve ...
Ubiquitin and Ub
... ubiquitin is the most highly conserved protein in eukaryotes and is not found in prokaryotes how can such a protein arise in eukaryotes only? Is there not an ancestral ubiquitin-like protein in prokaryotes? ubiquitinated proteins are recognized and degraded by the 26S proteasome in eukaryotes ...
... ubiquitin is the most highly conserved protein in eukaryotes and is not found in prokaryotes how can such a protein arise in eukaryotes only? Is there not an ancestral ubiquitin-like protein in prokaryotes? ubiquitinated proteins are recognized and degraded by the 26S proteasome in eukaryotes ...
protein synthesis - Science with Mrs Beggs
... – Translation of mRNA from DNA » Occors in the nucleus – Transcription of mRNA into a polypeptide chain » Occurs at the ribosome ...
... – Translation of mRNA from DNA » Occors in the nucleus – Transcription of mRNA into a polypeptide chain » Occurs at the ribosome ...
Symmetry in Protein Structures
... protein (or a subunit) consists of a number of amino acids (there are 20 types of them) connected into a linear chain. The sequence of amino acids specified a protein. For a protein to perform its function, it has to be folded into a three dimensional structure which then may be aggregated with othe ...
... protein (or a subunit) consists of a number of amino acids (there are 20 types of them) connected into a linear chain. The sequence of amino acids specified a protein. For a protein to perform its function, it has to be folded into a three dimensional structure which then may be aggregated with othe ...
post-transcription
... • One benefit of genes with introns is a phenomenon called alternative splicing • A pre-mRNA with multiple introns can be spliced in different ways – This will generate mature mRNAs with different combinations of exons ...
... • One benefit of genes with introns is a phenomenon called alternative splicing • A pre-mRNA with multiple introns can be spliced in different ways – This will generate mature mRNAs with different combinations of exons ...
Review Questions
... Quaternary means “fourth”. This level only occurs when there is more than one polypeptide in a protein. Composed of four polypeptides, hemoglobin is a good example. The individual polypeptides in the quaternary structures are joined to each other by bonds between the R-groups, just like the tertiary ...
... Quaternary means “fourth”. This level only occurs when there is more than one polypeptide in a protein. Composed of four polypeptides, hemoglobin is a good example. The individual polypeptides in the quaternary structures are joined to each other by bonds between the R-groups, just like the tertiary ...
14-3 The First Life Forms
... • Certain kinds of minerals formed a template on which organic molecules lined up to form polymers. • Self-replicating RNA began to evolve inside cell-like structures such as microspheres or coacervates. – The self-replicating RNA could have provided the hereditary information that the cell-like str ...
... • Certain kinds of minerals formed a template on which organic molecules lined up to form polymers. • Self-replicating RNA began to evolve inside cell-like structures such as microspheres or coacervates. – The self-replicating RNA could have provided the hereditary information that the cell-like str ...
RNA Processing
... assist with replication and/or packaging (Small RNAs associated with plant RNA viruses.) Segments of their RNA genome promote site-specific RNA cleavage reactions associated with replication ...
... assist with replication and/or packaging (Small RNAs associated with plant RNA viruses.) Segments of their RNA genome promote site-specific RNA cleavage reactions associated with replication ...
To the protocol
... Proteins are composed of one or several chains of amino acid, which fold into specific secondary structures. Three such structures we will examine closer are alphahelix, beta-pleated-sheet and loop. These structures position important amino acids in space, enabling their side chains to carry out the ...
... Proteins are composed of one or several chains of amino acid, which fold into specific secondary structures. Three such structures we will examine closer are alphahelix, beta-pleated-sheet and loop. These structures position important amino acids in space, enabling their side chains to carry out the ...
Organic Compounds Powerpoint
... When two sugars bind together via DEHYDRATION SYNTHESIS a disaccharide is formed. • glucose + glucose forms the sugar maltose • glucose + fructose forms the sugar sucrose • galactose + glucose forms the sugar lactose ...
... When two sugars bind together via DEHYDRATION SYNTHESIS a disaccharide is formed. • glucose + glucose forms the sugar maltose • glucose + fructose forms the sugar sucrose • galactose + glucose forms the sugar lactose ...
SR protein
SR proteins are a conserved family of proteins involved in RNA splicing. SR proteins are named because they contain a protein domain with long repeats of serine and arginine amino acid residues, whose standard abbreviations are ""S"" and ""R"" respectively. SR proteins are 50-300 amino acids in length and composed of two domains, the RNA recognition motif (RRM) region and the RS binding domain. SR proteins are more commonly found in the nucleus than the cytoplasm, but several SR proteins are known to shuttle between the nucleus and the cytoplasm.SR proteins were discovered in the 1990s in Drosophila and in amphibian oocytes, and later in humans. In general, metazoans appear to have SR proteins and unicellular organisms lack SR proteins.SR proteins are important in constitutive and alternative pre-mRNA splicing, mRNA export, genome stabilization, nonsense-mediated decay, and translation. SR proteins alternatively splice pre-mRNA by preferentially selecting different splice sites on the pre-mRNA strands to create multiple mRNA transcripts from one pre-mRNA transcript. Once splicing is complete the SR protein may or may not remain attached to help shuttle the mRNA strand out of the nucleus. As RNA Polymerase II is transcribing DNA into RNA, SR proteins attach to newly made pre-mRNA to prevent the pre-mRNA from binding to the coding DNA strand to increase genome stabilization. Topoisomerase I and SR proteins also interact to increase genome stabilization. SR proteins can control the concentrations of specific mRNA that is successfully translated into protein by selecting for nonsense-mediated decay codons during alternative splicing. SR proteins can alternatively splice NMD codons into its own mRNA transcript to auto-regulate the concentration of SR proteins. Through the mTOR pathway and interactions with polyribosomes, SR proteins can increase translation of mRNA.Ataxia telangiectasia, neurofibromatosis type 1, several cancers, HIV-1, and spinal muscular atrophy have all been linked to alternative splicing by SR proteins.