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Protein Folding File
Protein Folding File

... What are the two main structural motifs present in secondary folding of amino acid chains? What type of bonding stabilizes alpha helices and beta sheets? In addition to H-bonding, what type of bonding leads to stronger covalent bonds between amino acids? After secondary structures are formed, what i ...
Nucleic Acids and Protein Synthesis
Nucleic Acids and Protein Synthesis

... sugar, phosphate group and nitrogen bases) • It uses ribose as its sugar • Instead of using thymine, it uses uracil (A, U, G, C) • It is a single strand only ...
BioH From DNA to proteins
BioH From DNA to proteins

... • Promoter sequence on mRNA - signals “start” for transcribing DNA sequence into RNA sequence • ONE strand only – forming juvenile RNA • Uracil used instead of Thymine • Use Cytosine, Guanine, Adenine (same as DNA) ...
Biology 211 Intro Molecular and Cell Biology
Biology 211 Intro Molecular and Cell Biology

... tRNAs: Act as interpreters, converting nucleic acid information into a sequence of amino acids ...
Section 1.5 Name:
Section 1.5 Name:

... ii. Also,  RNA  does  not  have  thymine,  instead  it  has  the  pyrimidine  of  _______________   iii. RNA  is  only  a  _________________  strand  -­‐  DNA  is  a  double  strand   b. Types  of  RNA   i. _____________________  RNA  –   ...
Lh6Ch04bProt
Lh6Ch04bProt

... diseases depend on organ the fibers occur ...
Protein functions part 2 File
Protein functions part 2 File

...  A variety of different bonds stabilise the secondary and tertiary structures of proteins  Hydrogen bonds form between oxygen and hydrogen atoms within the main amino acid chain and between the R groups  Disulphide bridges form between sulphur atoms in the R groups of amino acids such as cytsein ...
Chapter 4
Chapter 4

... pictured as a helix with two residues per turn ...
From gene to protein 2
From gene to protein 2

... Exon size is somewhat uniform (averaging about 150 nucleotide pairs). Exon-intron boundaries are marked with spliceosome components ...
Name__________________________ Date______ Period
Name__________________________ Date______ Period

... 7. Do some amino acids have more than one codon? Give an example. 8. Name the start codon. 9. Name the 3 stop codons. 10. Define translation. ...
Repetitive Patterns in Proteins
Repetitive Patterns in Proteins

... Genetic Mechanisms: •  Replication slippage •  Illegitimate recombination •  Crossover during sexual recombination (“exon shuffling”) •  (Retro)-Transposition -> These processes result in novel domain compositions, circularly permuted proteins (includes loss), or repetitive proteins ...
Post-transcriptional gene control
Post-transcriptional gene control

... genes of protozoans • Group II self-splicing introns occur in chloroplasts and mitochondria of plants and ...
Molecules of Life MBBS Prof. Fridoon
Molecules of Life MBBS Prof. Fridoon

... Proteins: Structure Primary Structure: the sequence of amino acids bonded by peptide linkages (Diversity 20n) Secondary Structure: α helices and β pleated sheets (maintained by hydrogen bonds between atoms of the amino acid residues) ...
Chapter 11 DNA and Genes
Chapter 11 DNA and Genes

... • Makes up the ribosome. The ribosome binds to mRNA and uses the instructions to hook together amino acids into long chains that will become proteins. ...
Making Proteins - Foothill Technology High School
Making Proteins - Foothill Technology High School

... Steps of DNA Transcription Making mRNA from DNA 1. Helicase unzips DNA at the gene of interest 2. RNA polymerase matches RNA nucleotide bases to DNA, using one side as a template. 3. The mRNA strand is created. It now compliments the original DNA strand (G-C and A-U). 4. Ligase helps the strand of ...
Protein Folding and Quality Control
Protein Folding and Quality Control

... binds to nascent unfolded polypeptide 2)ATP hydrolyzed and HSP form hydrophobic pockets, allows for normal folding of hydrophobic elements. 3+4) When ATP reassociates, goes back to original configuration and folded protein is released. GroEL : acts as bacterial chaperonin (large macromolecular machi ...
Proteins - Mr Waring`s Biology Blog
Proteins - Mr Waring`s Biology Blog

... A protein consists of one or more polypeptide chains folded into a highly specific 3D shape. There are up to four levels of structure in a protein: primary, secondary, tertiary and quaternary. Each of these play an important role in the overall structure and function of the protein. 7 of 29 ...
PROTIEN SYNTHESIS
PROTIEN SYNTHESIS

... The RNA that is a permanent structural part of a ribosome. ri·bo·some A minute round particle composed of RNA and protein that is found in the cytoplasm of living cells and serves as the site of assembly for polypeptides encoded by messenger RNA pro·tein Any of a group of complex organic macromolecu ...
Document
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... Alternative RNA splicing --- One exon codes for one domain of a protein (p. 336) Introns allow for more crossing over without disrupting domain coding = new proteins sequences. ...
Asymptotics of RNA Shapes: secondary structure
Asymptotics of RNA Shapes: secondary structure

... models and novel algorithms to solve fundamental problems of molecular biology in the post-genome era. A central problem of structural biology concerns the algorithmic prediction of the structure of RNA and protein from only the nucleotide resp. amino acid sequence. In the context of RNA, nucleotide ...
Model Description Sheet
Model Description Sheet

... pathway, small RNAs derived from viruses are used by Ago-2 to slice virus mRNA, protecting the cells from infection. In the miRNA pathway, Ago-2 utilizes naturally occurring miRNA to slice cellular mRNAs to control protein production. Ago-2 works by binding small (~22 nucleotide) regulatory RNAs (si ...
Chapter 5 - Richsingiser.com
Chapter 5 - Richsingiser.com

... homologues – Conserved residue – similar (class) aa among homologues – Hypervariable residue – no similarity among homologues ...
Slide ()
Slide ()

... COPII vesicles to the cis-Golgi (anterograde transport). Movement of proteins through the Golgi appears to be mainly by cisternal maturation. In the TGN, the exit side of the Golgi, proteins are segregated and sorted. Secretory proteins accumulate in secretory vesicles (regulated secretion), from wh ...
Slide ()
Slide ()

... COPII vesicles to the cis-Golgi (anterograde transport). Movement of proteins through the Golgi appears to be mainly by cisternal maturation. In the TGN, the exit side of the Golgi, proteins are segregated and sorted. Secretory proteins accumulate in secretory vesicles (regulated secretion), from wh ...
PTM
PTM

... specific codon-encoded amino acids into more than 100 variant amino acids with new properties. These, and a number of other modifications, can considerably increase the information content and functional repertoire of proteins ...
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LSm



In molecular biology, LSm proteins are a family of RNA-binding proteins found in virtually every cellular organism. LSm is a contraction of 'like Sm', because the first identified members of the LSm protein family were the Sm proteins. LSm proteins are defined by a characteristic three-dimensional structure and their assembly into rings of six or seven individual LSm protein molecules, and play a large number of various roles in mRNA processing and regulation.The Sm proteins were first discovered as antigens targeted by so-called Anti-Sm antibodies in a patient with a form of Systemic lupus erythematosus (SLE), a debilitating autoimmune disease. They were named Sm proteins in honor of Stephanie Smith, a patient who suffered from SLE. Other proteins with very similar structures were subsequently discovered and named LSm proteins. New members of the LSm protein family continue to be identified and reported.Proteins with similar structures are grouped into a hierarchy of protein families, superfamilies, and folds. The LSm protein structure is an example of a small beta sheet folded into a short barrel. Individual LSm proteins assemble into a six or seven member doughnut ring (more properly termed a torus), which usually binds to a small RNA molecule to form a ribonucleoprotein complex. The LSm torus assists the RNA molecule to assume and maintain its proper three-dimensional structure. Depending on which LSm proteins and RNA molecule are involved, this ribonucleoprotein complex facilitates a wide variety of RNA processing including degradation, editing, splicing, and regulation.Alternate terms for LSm family are LSm fold and Sm-like fold, and alternate capitalization styles such as lsm, LSM, and Lsm are common and equally acceptable.
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