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... Has polarity with an amino group one end (Nterminus) and a carboxyl group on the other (C-terminus). Has a backbone of repeating N-C-C-N-C-C Polypeptide chains range in length from a few monomers to more than a thousand, and a unique linear sequence of amino acids. ...
Understanding DNA
Understanding DNA

... information about making protein.  Unfortunately, DNA is too huge to leave the nucleus but the protein is made in the ribosomes.  DNA is too important to cellular function to risk damage in the cytoplasm ...
4 slides pdf
4 slides pdf

... • protease cleaves protein into small peptides; then ionized, analyzed in mass spectrometer (determines the mass-tocharge ratio of each peptide). • mass spectrum compared to database of known spectra ...
ppt
ppt

... Water molecules form hydrogen bonds: with each other, or with other polar molecules Hydrophilic molecules (ions, polar) are soluble Hydrophobic molecules (nonpolar) are not soluble Organic molecules: ...
Gene expression and regulation
Gene expression and regulation

... when and where specific genes are activated and the amount of protein or RNA product produced. Some genes are expressed continuously, as they produce proteins involved in basic metabolic functions; some genes are expressed as part of the process of cell differentiation; and some genes are expressed ...
SURVEY OF BIOCHEMISTRY
SURVEY OF BIOCHEMISTRY

... SURVEY OF BIOCHEMISTRY Transcription and Translation ...
Transcription and the Central Dogma
Transcription and the Central Dogma

... from many genes averages out to this. – The closer these 2 regions actually are to the consensus sequences, the “stronger” the promoter, meaning the more likely RNA polymerase binding and transcription will occur. ...
Ribosomes and In Vivo Folding
Ribosomes and In Vivo Folding

... In mammals, clearly folding and chain association f (extent of hydroxylation). But! Collagens from cold-blooded creatures have very low levels of hydroxyproline; yet still form collagen, still Tm f {proline rings} Triple helix driven at low temp by glycines and prolines Driven at high temperature b ...
protein synthesis
protein synthesis

... There are 4 bases (A, T, C, G) Thus 4 3 (64) possible combinations of codons There are 20 amino acids Code is redundant (2 or more codons code for same amino acid) but not ambiquous (no codon codes fro more than 1 amino acid) ...
Outline of MALDI mass spectrometric analysis
Outline of MALDI mass spectrometric analysis

... If the protein is identified as "unknown", the sequences obtained by mass spectrometry can be used to query EST and genomic databases. The identified nucleotide sequences can then be used for cloning the gene. ...
FoldIndex©: a simple tool to predict whether a given protein
FoldIndex©: a simple tool to predict whether a given protein

... The web tool FoldIndex© , implementing the original Uversky algorithm, provides a single score for the entire sequence, predicting whether it is folded or not. The other methods calculate a separate fold score for each individual residue. In order to compare the various methods we obtained a fold sc ...
No Slide Title
No Slide Title

... Special Features of Protein-Protein Interfaces • Critical for macromolecular recognition • Typically, ca. 500 - 1500 Å2 of surface buried upon complex formation by two globular proteins • Epitopes on protein surface thus may have a “hybrid” character, compatible with both a solvent-exposed (‘free”) ...
DNA transcription
DNA transcription

... information embedded in DNA and RNA into ordered amino acids and proteins is the genetic code. And every living organism uses the same genetic code. The genetic code consists of the sequence of nitrogen bases—A, C, G, U—in an mRNA chain. The four bases make up the “letters” of the genetic code. The ...
Proteome analysis of Arabidopsis thaliana mitochondrial proteins
Proteome analysis of Arabidopsis thaliana mitochondrial proteins

... Some 95% of the genes encoding mitochondrial proteins are located in the nucleus and the proteins are targeted back to the mitochondrion using encrypted targeting information in the protein sequence. Identification of all genes carrying these targeting sequences is one way of defining the complete s ...
Principle_files/6-Translation n
Principle_files/6-Translation n

... The dogma is a framework for understanding the transfer of sequence information between sequential information-carrying biopolymers, in the most common or general case, in living organisms. There are 3 major classes of such biopolymers: DNA and RNA (both nucleic acids), and protein. There are 3×3 = ...
TRANSCRIPTION TRANSLATION
TRANSCRIPTION TRANSLATION

... by mRNA is called translation.  Involves:  (i) charging of the tRNA with the specific amino acids and  (ii) synthesis of polypeptide chain by the ribosomes. ...
DNA vs. RNA
DNA vs. RNA

...  Similar signals in DNA cause transcription to stop when the new RNA molecule is completed. ...
File
File

...  Channel proteins transport water soluble substances, especially the ions or very small molecules from one side of the membrane to the other side according to concentration  this process is known as diffusion b- Carrier proteins:  Carrier proteins change their shape to transport certain molecules ...
Bioinformatics in Computer Sciences at NJIT
Bioinformatics in Computer Sciences at NJIT

... consisting of four letters: A, C, G, and T. They could be very long, e.g. thousands and even millions of letters • Proteins are also represented as strings of 20 letters (each letter is an amino acid). Their 3-D structure determines the function to a large extent. ...
Biomolecules
Biomolecules

... A Protein (PROH teen) is a large molecule formed by linked smaller molecules called amino acids. ...
Messenger RNA (mRNA)
Messenger RNA (mRNA)

... Ribosomal RNA (rRNA): produced in the nucleus, makes up part of the ribosomes. Ribosomes are the site of protein synthesis. Transfer RNA (tRNA): shuttles amino acids to the ribosomes. It's responsible for bringing the correct amino acids into place at the appropriate time. It does this by reading th ...
gida bi̇yoteknoloji̇si̇-2
gida bi̇yoteknoloji̇si̇-2

... called as -35 position. promoter sequence is not transcribed. • There are two specific sequence (consensus sequences) on the promoter region which provide the recognition and binding of the enzyme to the promoter for the initiation of the transcription. These are:  5’-TTGACA-3’ is in the -35 positi ...
Student work sheets for Power Point Slides
Student work sheets for Power Point Slides

... 13) The protein structure is three dimensional because of the folding of the amino acids. 14) Endoplasmic reticulum is located outside the nucleus. 15) An anticodon consists of three base pairs which are opposite to the base pairs in the mRNA. Slide 4 16) Describe what you see from this slide. Slide ...
Techniques in Protein Biochemistry
Techniques in Protein Biochemistry

... Antibodies are used as a reagent to determine the amount of a protein or other antigen present. Enzyme-linked immunosorbent Assay (ELISA) quantifies the amount of protein present because the antibody is linked to an enzyme whose reaction yields a readily identified colored product. ...
Outline Visualizing proteins with PyMol
Outline Visualizing proteins with PyMol

... Classifying Ter/ary Structure Historically: Much work done by Chothia to develop rules governing packing arrangements of secondary structure (like ridge-into-groove model for helix-helix packing) Modern schemes use sequence similarity and structurestructure comparisons to organize the protein ...
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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.
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