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Nutrition
Nutrition

... What name is given to fats that are liquid at room temperature? ………………………. State two functions of fats in the human body An example of a fat-soluble vitamin is …………………………………………………. A good source of this vitamin is ………………………………………………………... A lack of this vitamin may lead to ……………………………………………………… ...
Group 6 - Purdue Genomics Wiki
Group 6 - Purdue Genomics Wiki

... •Good E-value •Proper splice sites •Both program agreed •No mobile elements ...
Group 6
Group 6

... disulfide bonds. We can denature the proteins by disrupting the H-bonds that are within the structure. When this happens the overall shape of the protein changes and new properties can be observed. The shape of a protein is associated with food processing properties, such as solubility, gel formatio ...
Chapter 21 Biosynthesis of amino acids, nucleotides and related
Chapter 21 Biosynthesis of amino acids, nucleotides and related

Three main topics for this Intro lecture
Three main topics for this Intro lecture

... good news . . . but what, exactly, does it mean? • A match indicates that your sequence has the domain structure . . . but does it also have the function? • You cannot say before looking into these details: • Where are the catalytic residues on the domain? • Does your sequence have the right residue ...
Packet 2 - w/answers
Packet 2 - w/answers

... Amino acids have ___amino_____ and ____carboxyl______ groups. They are made unique by the “R” group that is attached to carbon “R” is like a variable in algebra class. It can have many values (structures). The Function of the amino acid is determined by the structure and conformation of the “R” grou ...
Proteins | Principles of Biology from Nature Education
Proteins | Principles of Biology from Nature Education

... cells in the body. Researcher Eric Gouaux and his colleagues at Oregon Health Sciences University recently completed a map of a complex and very important brain receptor called the glutamate receptor. Binding of the neurotransmitter glutamate, an amino acid, to the glutamate receptor (itself a prote ...
Mouse anti-receptor protein tyrosine phosphatase sigma, RPTPσ
Mouse anti-receptor protein tyrosine phosphatase sigma, RPTPσ

... proteins that are involved in axon growth and guidance during neural development. Members of this subfamily, RPTPσ, RPTPδ and LAR contain two cytoplasmic phosphatase domains and extracellular immunoglobulin domains followed by fibronectin type III repeats. RPTPσ is a type I transmembrane protein tha ...
LABORATORY DIAGNOSIS OF PROTHROMBOTIC STATES
LABORATORY DIAGNOSIS OF PROTHROMBOTIC STATES

... Increased prothrombin synthesis seen (> 115% of normal) Implicated in both arterial (stroke) and venous thrombosis as well as pregnancy-related thrombosis ...
Proteomics
Proteomics

... – The digestion enzyme is Trypsin, with 0 missed cleavages – The result is a list of theoretical peptides that can be compared to the measured masses ...
Lab Activity 1
Lab Activity 1

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MTC15 - toddgreen
MTC15 - toddgreen

... glucose which is found in liver, muscle and brain cells and is used a mid-term storage polymer (e.g. overnight) The extra-cellular matrix within which all our bodies’ cells reside is composed of hyaluronic acid which carries a negative charge in solution, thus attracting sodium which in turn attract ...
Biomolecules
Biomolecules

... Side chains of polar (hydrophilic) a.a. can participate in hydrogen or ionic bonds. Therefore, in aqueous environment polar a.a. tend to be present on the surface of proteins. Polar (hydrophilic) amino acids are classified into: - Polar charged amino acids include ...
SUBUNITS FROM REDUCED .AND S
SUBUNITS FROM REDUCED .AND S

... organization of the protein. Rutner and Lane (1967) dissociated the protein with sodium dodecyl sulphate and isolated, by gel filtration, two subunits having different electrophoretic mobilities, sedimentation velocities, and amino acid compositions. Sugiyama and Akazawa (1967) also observed multipl ...
No Slide Title
No Slide Title

... 3 Types of RNA: 1) Messenger RNA (mRNA): brings information from the DNA in the nucleus out to the ribosomes; 2) Ribosomal RNA (rRNA): clamp on to the mRNA and use its information to assemble amino acids into a protein; 3) Transfer RNA (tRNA): the “supplier”; transports amino acids to the ribosome ...
Biochemistry Biochemistry is a science concerning the chemical
Biochemistry Biochemistry is a science concerning the chemical

... both the polarity and the structural features of their side chains (e. g. polar, nonpolar; aliphatic, aromatic; sulfur-containing; charged, uncharged; acidic, basic). The amphoteric properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4-hydroxyprolin ...
Does intracrine amplification provide a unifying principle for the
Does intracrine amplification provide a unifying principle for the

... plaques or dying cells. The trafficking of misfolded proteins in nanotubes has been suggested. So there are commonalities between intracrine action and the actions of misfolded neural proteins. A frequent feature of intracrine networks which potentially informs the understanding of TSEs, and therefo ...
Biochemistry Biochemistry is a science concerning the chemical
Biochemistry Biochemistry is a science concerning the chemical

... according to both the polarity and the structural features of their side chains (e. g. polar, nonpolar; aliphatic, aromatic; sulfur-containing; charged, uncharged; acidic, basic). The amphoteric properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4- ...
Biochemistry Biochemistry is a science concerning the chemical
Biochemistry Biochemistry is a science concerning the chemical

... both the polarity and the structural features of their side chains (e. g. polar, nonpolar; aliphatic, aromatic; sulfur-containing; charged, uncharged; acidic, basic). The amphoteric properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4-hydroxyprolin ...
PPT2
PPT2

... The catalysis of all biochemical reactions is done by enzymes, which contain protein. ...
3.5 What are the chemical structures and functions of nucleic acids?
3.5 What are the chemical structures and functions of nucleic acids?

... The unique function of the nucleic acids—DNA and RNA—is information storage; they form the hereditary material that passes genetic information to the next generation. Nucleic acids are polymers of nucleotides. A nucleotide consists of a phosphate group, a pentose sugar (ribose in RNA and deoxyribose ...
lecture notes-molecular biology-web
lecture notes-molecular biology-web

... Polyadenylation: a string of adenine nucleotides are added to the 3’ end. The string is several hundred nucleotides long. These two modifications are thought to increase mRNA stability and facilitate transport across the nuclear membrane. ...
Chemical Basis of Life packet #2
Chemical Basis of Life packet #2

... o Higher concentration of substrate means more substrate finding the active site. o Production speeds up. ...
Unit 2 - Part 1
Unit 2 - Part 1

... Why do organisms need enzymes?  Reactions occur very slow on their own  Enzymes speed up reactions 2. How are enzymes specific?  They have a specific shape that only allows them to work on specific substrates. ...
Protein Structure Prediction
Protein Structure Prediction

... ref|XP_001160877.1| PREDICTED: zinc finger protein 227 isoform 1... ref|XP_001132303.1| PREDICTED: similar to zinc finger protein 43... ref|XP_001166123.1| PREDICTED: zinc finger protein 607 isoform 4... sp|Q8IYB9|ZN595_HUMAN Zinc finger protein 595 >gi|23271315|gb|AA... ref|XP_523409.2| PREDICTED: ...
< 1 ... 464 465 466 467 468 469 470 471 472 ... 693 >

Proteolysis



Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.
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