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Special aspects of renal metabolism
Special aspects of renal metabolism

...  Removing α-amino group is obligatory in the catabolism of all amino acids  Once removed, nitrogen can be incorporated into other compounds or excreted, with the carbon skeletons metabolized  Transamination and oxidative deamination will provide ammonia and aspartate (sources of urea nitrogen) ...
abstract
abstract

... formaTon  is  that  oxygen  demand  is  derived  from  seVling  biogenic   parTcles  via  high  biological  producTvity  in  surface  waters.    The   hypothesis  that  freshly  seVled  parTcles  in  sediments  parTcipate   acTvely  in  bio ...
Introduction to Biology
Introduction to Biology

... reconverted into RNA by enzymatic means. Viral propagation and replication were accomplished by throwing the virus into a predesigned protein soup that contained all the polymerases and other enzymatic ingredients necessary for RNA transcription and translation. The synthetic virus was able to succe ...
DNA PROTEIN
DNA PROTEIN

... • WHY CAN’T PROTEINS JUST BE TRANSLATED RIGHT FROM DNA? – Using RNA provides protection for DNA & its info – Using RNA allows more protein copies to be made at the same time – BLUEPRINT EXAMPLE ...
Enzymes are catalysts in living things
Enzymes are catalysts in living things

... called active sites. ...
Macromolecule Basics
Macromolecule Basics

... • Organic molecules are the molecules which exist in all living things. • They are life’s building blocks. • All organic things are formed from these organic molecules. • There are four categories of organic molecules: ...
The Macromolecule Worksheet
The Macromolecule Worksheet

... 15. How many amino acids can your body make? Where do you get the rest of them? 16. Name the special bond that holds proteins together. 17. What determines a protein’s structure and function? 18. How are hydrogen bonds involved in the structure of a protein? Nucleic Acids: 19. What is the job of a n ...
Camp 1 - University of California, Santa Cruz
Camp 1 - University of California, Santa Cruz

... Lipid ...
* Abundant! * Able to share 4 outer valence electrons! * Versatile
* Abundant! * Able to share 4 outer valence electrons! * Versatile

... • Single amino acids are bonded together using peptide bonds. • EX: Meat, eggs, fish ...
1. Which of the following is not a feature of scientific hypotheses? A
1. Which of the following is not a feature of scientific hypotheses? A

An overview of biochemistry for bioCHEM480
An overview of biochemistry for bioCHEM480

... 1. The  Cell.     The  cell  is  the  fundamental  unit  of  life.  Cells,  whether  they  be  unicellular  or   multi-­‐cellular  organisms,  must  operate  as  "open"  thermodynamic  systems  by  establishing  a   dynamic  equilibrium  w ...
Protein Folding and The Impact of Mutations
Protein Folding and The Impact of Mutations

... When amino acids are assembled in a line to make a protein, they do not stay in an even, straight line. This is similar to a line at lunch sometimes… A couple might move closer to each other without leaving the line  Two friends fighting might move away from each other  That one kid who really lik ...
Chapter 2.3: Carbon Compounds
Chapter 2.3: Carbon Compounds

... Enzymes are catalysts. c. Enzymes provides a site (called the active site) where reactants can be brought together to react. This decreases the activation energy d. In a reaction involving an enzyme, the reactants are called substrates e. Enzymes can be reused, but can only have one type of substra ...
Name Period ______ Date Chem/Biochem Test Study Guide
Name Period ______ Date Chem/Biochem Test Study Guide

... 27. A polymer of a protein is called a polypeptide. 28. An amino acid has three parts. What are they called? a. Amino group b. Carboxyl group c. R group 29. Briefly describe what happens in each structure of protein folding. a. Primary – Chain of amino acids by peptide bonds. b. Secondary – Hydrogen ...
Chemistry 202 Amino Acids, Peptides, and
Chemistry 202 Amino Acids, Peptides, and

... or drawn as zwitterion and would be named seryl-alanyl-glycine (Ser-Ala-Gly). It is clear that when 100 or more amino acids are involved and each of these may have one of 20 different structures, the number of possible proteins is huge. Some commonly occurring peptides are antibiotics, hormones, and ...
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5-Premedical-Molec-bas-of-inh

Amino Acids and Peptides-chap 3
Amino Acids and Peptides-chap 3

...  L-amino acids are found in all proteins; Damino acid image found in proline  D-amino acids are found in nature  Three letter or one-letter codes – refer to amino acids ...
Primary Structure
Primary Structure

... have a phosphate group. Phosphorylation is critical for many enzymes to work and affects quaternary folding so this will be looked at. Interestingly, the pI and Mw of the protein were calculated based solely on the primary amino acid sequence given and inputted to a calculator [3]. The results can b ...
Chapter 6 - Education Reformation
Chapter 6 - Education Reformation

Instructions for Biochemistry
Instructions for Biochemistry

... Life is 3-D The name and abbreviation(s) for the molecule are at the top of the card. An atom by atom picture of the molecule is in the middle of the card. You will build what you see in the picture, but remember that the picture is 2-D, and real life is 3-D! Use what you know about molecular archit ...
page 74-81
page 74-81

tRNA
tRNA

... Exonuclease degrade from 3’ to 5’ ...
FPG Summary
FPG Summary

... - Cystine has sulfhydryl (thiol) group which allows it to form disulphide bonds - Lysine is an essential amino acid - Protein structure levels: • primary —> linear amino acid sequence • secondary —> α-helix and β-sheets • tertiary —> polypeptide chain of α-helix and β-sheets • quaternary —> having 2 ...
Organic Compounds
Organic Compounds

... • Most of the useful behavior of organic compounds comes from functional groups attached to the carbons. A functional group is a special cluster of atoms that performs a useful function. ...
Macromolecules of Life
Macromolecules of Life

... • Consists of one or more polypeptides folded, coiled, and twisted into a specific 3D shape • Proteios – “first place” • There are many different shapes of proteins depending on its FUNCTION ...
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Biosynthesis



Biosynthesis (also called biogenesis or anabolism) is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined together to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides.The prerequisite elements for biosynthesis include: precursor compounds, chemical energy (e.g. ATP), and catalytic enzymes which may require coenzymes (e.g.NADH, NADPH). These elements create monomers, the building blocks for macromolecules. Some important biological macromolecules include: proteins, which are composed of amino acid monomers joined via peptide bonds, and DNA molecules, which are composed of nucleotides joined via phosphodiester bonds.
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