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Macromolecules For Identification
Macromolecules For Identification

... different amino acids that combine to form polypeptides (proteins). • The different amino acids are similar in structure. • The different amino acids have different side chain, but are otherwise identical. • Proteins have many important roles in organisms. Structural proteins such as collagen or ela ...
Nucleic Acids - One Day Enrichment
Nucleic Acids - One Day Enrichment

Introduction to Metabolism
Introduction to Metabolism

... Denitrifying Bacteria - reduce nitrates into ammonia. ...
Biology 12
Biology 12

MACROMOLECULE WEBQUEST
MACROMOLECULE WEBQUEST

... What is the ratio of Carbon to Hydrogen to Oxygen? ________ Carbohydrates comprise what percentage of our body cells? ________ List 4 monosaccharide ...
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 ...
Biochemistry Biochemistry is a science concerning the chemical
Biochemistry Biochemistry is a science concerning the chemical

... The formation, structure and properties of the peptide bond. Some important peptides in the human organism (glutathione, peptide hormones). The insulin synthesis. The classification of proteins according to their structure, properties and functions. The characteristics of primary, secondary, tertiar ...
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 ...
AArest
AArest

... methionine synthase This enzyme exists in humans but its activity is low and ...
Amino Acids
Amino Acids

... e.g. Cysteine and Methionine. Cystine,not involved in proteins. It is dimer of cysteine linked by S-S bond(oxidized form) ...
A Supramolecular Peptide Synthesizer
A Supramolecular Peptide Synthesizer

... after reaction with the activated amino acids. The condensation domain (C-domain) finally catalyzes the formation of the peptide, similar to the ribosome in RPS. Nevertheless, several differences between the two biosynthetic pathways are apparent. For instance, nonribosomal peptides (NRPs) are not r ...
103 final rev worksheet key
103 final rev worksheet key

... The induced-fit model allows for the broader specificity seen in some enzymes. It says that the active site and the substrate adjust their shapes to fit each other upon binding. Once the fit is achieved, the substrate is properly lined up for catalysis (its shape may also closely resemble the trans ...
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Ribosomes and The Golgi Apparatus
Ribosomes and The Golgi Apparatus

... Apparatus ...
Pipecleaner Proteins Lab
Pipecleaner Proteins Lab

... If your project was late, describe why ...
Organic Chemistry for Biology
Organic Chemistry for Biology

... Sometimes adding more concentration has little or no effect ...
Default Normal Template - Philadelphia University Jordan
Default Normal Template - Philadelphia University Jordan

... c. Denatured proteins are enzymatically inactive. d. Native proteins have enzymatic activity. e. Refolding of RNase was directed by the primary sequence. 4 Select the amino acid that has around α-carbon only one bond that can freely rotate: A. Valine B. Serine C. Glutamine D. Proline E. Asparagine 5 ...
amino-terminal
amino-terminal

... In addition, the nitrogen atom of a Pro residue in peptide linkage has no substituent hydrogen to participate in hydrogen bonds with other residues. ...
EXAM2
EXAM2

Fatty acid breakdown
Fatty acid breakdown

... Attachment of upper ligand is second example of triphosphate liberation from ATP • Cobalamin  Coenzyme B12 The other such reaction where this is observed is formation of Ado-Met ...
3.the nature of proteins
3.the nature of proteins

... called amino acids  Every amino acid possesses an amino end and a carboxylic acid end  There are twenty different naturally occurring amino acids  Amino acids differ by virtue of the nature of their R groups  Amino acids bond together forming peptide bonds  When two amino acids bond during a co ...
Exam 4 KEY
Exam 4 KEY

... 13. (5 pts) Explain why tyrosine is considered a non-essential amino acid even though humans lack the enzymes required for de novo tyrosine biosynthesis. Tyrosine is considered a non-essential amino acid because humans contain an enzyme (phenylalanine hydroxylase) that converts the essential amino a ...
Pipe Cleaner Protein Modeling C. Kohn, Waterford WI Name: Hour
Pipe Cleaner Protein Modeling C. Kohn, Waterford WI Name: Hour

... If your project was late, describe why ...
Rock Pocket Mouse Activity Trio
Rock Pocket Mouse Activity Trio

... addition, this change could increase the activation of the G protein without the need of a ligand. This increase in activation would amplify the levels of cAMP, thus increasing eumelanin production. c. The normal receptor conformation requires a ligand for activation of the G protein. If the ligand ...
Organic Compounds: Carbohydrates
Organic Compounds: Carbohydrates

... -COOH (carboxyl) group – allow them to act as acids -NH2 (amine) group – gives basic properties R-group – what is different for each that makes them chemically unique ...
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Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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