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Leptin is a 16 kDa, 146 amino acid residue non
Leptin is a 16 kDa, 146 amino acid residue non

... or -20 °C. Avoid repeated freezing and thawing. More dilute solutions stored at -20 °C will lose activity faster. About Rat Leptin: Leptin is a 16 kDa, 146 amino acid residue non-glycosylated protein hormone involved in regulating body weight, metabolism and reproductive function. It is encoded by t ...
Name 1 BIO 451 14 December, 1998 FINAL EXAM
Name 1 BIO 451 14 December, 1998 FINAL EXAM

Poster
Poster

... shape. With the help of guanine nucleotide exchange factors (GEFs) and GAP proteins, Rap1b then binds to an effector protein, activating integrins, which control the attachment of cells to matrix proteins. In turn, the activated integrins located on the cell membrane of a platelet allow platelets to ...
Solvil - Vitaflo UK
Solvil - Vitaflo UK

... Indications Solvil is for use in the dietary management of urea cycle disorders or other inborn errors of metabolism requiring branched chain amino acid (BCAA) supplementation. Dosage and Administration To be determined by the clinician or dietitian and is dependent on the age, bodyweight and medica ...
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File

... – RNA may fold back on itself to form complex three dimensional structures, as in ribosomes. – RNA may have catalytic activity; such RNA enzymes are called ribozymes. – Adenosine triphosphate (ATP) is a nucleotide that plays a key role in cellular metabolism, whereas guanosine triphosphate (GTP) ser ...
Carbohydrate Fans
Carbohydrate Fans

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Algebra 1 - Edublogs
Algebra 1 - Edublogs

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Chapter 3 Overview - Greensburg.k12.in.us
Chapter 3 Overview - Greensburg.k12.in.us

... dehydration synthesis (condensation reaction). During dehydration synthesis, a hydroxyl (OH) group is removed from one monomer and a hydrogen is removed from the other to join them together to form a polymer. During this process, water is produced (see left). ...
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Nutrients - FTHS Wiki

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Do Now - Montville.net

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PracticeFinalSP2003

... c) if R represents a H atom, the amino acid is called glycine (gly),. Draw the molecule and tell me if glyciene an enantiomer. If it does, mark with an asterisk (*) the chiral carbon and draw the enantiomer. d) if R represents a methyl group (-CH3), then the amino acid is called alanine (ala). Draw ...
Exam 1 SQ Key Chapter 2: Water and Carbon—The Chemical Basis
Exam 1 SQ Key Chapter 2: Water and Carbon—The Chemical Basis

... 7.) Is the directionality of AA arranged CN terminus or NC terminus? a. NC 8.) Describe the flexibility of the peptide backbone. a. Peptide bond has partial double bond character which limits free rotationthe bonds directly adjacent to the alpha carbon have some rotation 9.) Explain the four lev ...
ch 6 group review
ch 6 group review

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Connect the dots…DNA to Disease, Oltmann
Connect the dots…DNA to Disease, Oltmann

... search against a database of known proteins to determine which protein their sequence encodes. The goal is to show students that genes encode proteins, which in turn can cause disease if mutated or function improperly. Background Unfortunately, most students fail to make the connection between DNA s ...
Connect the dots…DNA to Disease, Oltmann
Connect the dots…DNA to Disease, Oltmann

... search against a database of known proteins to determine which protein their sequence encodes. The goal is to show students that genes encode proteins, which in turn can cause disease if mutated or function improperly. Background Unfortunately, most students fail to make the connection between DNA s ...
Degradation signals within both terminal domains of the cauliflower
Degradation signals within both terminal domains of the cauliflower

... Protein degradation plays an important role in many cellular processes: it allows much faster alteration of the amount of regulatory proteins than transcriptional or translational regulation, and is important for the relocation of biochemical resources. Although protein degradation has not been exte ...
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Healthy or ill: Just a single wrong fold - Reizende DNA-labs

... As stated before, the spatial structure of a protein is of great importance to its function, so it is useful to be able to show it. Namely, how would you know that something has changed in a structure when you don’t know what the structure is? Even if you have visualized the structure of a protein i ...
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Human Physiology

... • The hydrolysis of starch is done by amylases. With the aid of an amylase (such as pancreatic amylase), water molecules enter at the 1 -> 4 linkages, breaking the chain and eventually producing a mixture of glucose and ...
Lect1.AAs.Peptides.pH.pK
Lect1.AAs.Peptides.pH.pK

... Asn is amidated version of Asp Gln is amidated version of Gln Asn and Gln are NOT charged, but are higly polar NH2 group on Gln in proteins can be site for carbohydrate addition (N-linked glycosylation) ...
THE STRUCTURE AND FUNCTION OF MACROMOLECULES
THE STRUCTURE AND FUNCTION OF MACROMOLECULES

... • Show ambivalent behavior towards water. Hydrocarbon tails are hydrophobic, and the polar head (phosphate group with attachments) is hydrophilic. • Cluster in water as their hydrophobic portions turn away from water. One such cluster, a micelle, assembles so the hydrophobic tails turn towards the w ...
Word file - UC Davis
Word file - UC Davis

... If this table is called T, T(i,j) represents the number of time that amino acid i is replaced with amino acid j (for example there are 100 mutations F-> Y). You have doubts however and you think that you have made some mistakes. What is the most likely hint that makes you think that this table is wr ...
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Question 2: Multiple-Choice Standard: Chemistry of Life

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Quiz: DNA, RNA and Protein

... 11. What kind of bond holds the DNA bases together? 12. A three nucleotide sequence of DNA is called a _______________. 13. How many different amino acids are there? 14. State three differences between DNA and RNA. 15. The base uracil pairs with what DNA nucleotide 16. If the DNA coding strand is GT ...
Chemical Basis of Life
Chemical Basis of Life

... o Higher concentration of substrate means more substrate finding the active site. o Production speeds up. ...
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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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