BIOL 2000 Lecture Notes - Hydrogen Bond, Ribosome, Protein Structure

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Published on 12 Apr 2013
School
UofL
Department
Biology
Course
BIOL 2000
Chapter 9-1
Proteins and their synthesis
Protein synthesis occurs through the process called translation
Translation occurs on RNP particles called ribosomes
Year 2000-First high result ion 3D structures solved for ribosomes
o How does the ribosome work?
o How is the ribosome inhibited- antibiotics?
Translation components
Ribosome- large RNP complex
o Catalyzes peptide bond formation
Transfer RNAs- tRNAs
o Non coding RNAs
o Bring amino acids to the ribosome
o Decode information on the mRNA
Messenger RNAs (mRNAs)
o Template for protein synthesis
Protein structure
Amino acids with different properties
Protein sequence and 3D shape influences function
o Molecules can be bound
o Cellular location
o Protein-protein interactions
Shape affects type of molecules proteins can bind to and work
with
Protein 3D structure is stabilized by:
o Ionic interactions
o Hydrogen bonding (H-bonds)
o Hydrophobic interactions and Van der Waals forces
Each individual bond is weak but add them up and it gives
protein their structure
Amino Acids structure
There are 20 different standard amino acids in
proteins
Side chain R group is different for each one
Different R group properties
o Charged (+ or -)
o Hydrophobic
o Hydrophilic
o Aromatic
Planar ring structures
Chain of amino acids are linked by peptide bonds
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Document Summary

Protein synthesis occurs through the process called translation. Translation occurs on rnp particles called ribosomes. Ribosome- large rnp complex: catalyzes peptide bond formation. Transfer rnas- trnas: non coding rnas, bring amino acids to the ribosome, decode information on the mrna. Messenger rnas (mrnas: template for protein synthesis. Protein sequence and 3d shape influences function: molecules can be bound, cellular location, protein-protein interactions. Shape affects type of molecules proteins can bind to and work. Protein 3d structure is stabilized by: with: ionic interactions, hydrogen bonding (h-bonds, hydrophobic interactions and van der waals forces. Each individual bond is weak but add them up and it gives protein their structure. There are 20 different standard amino acids in proteins. Side chain r group is different for each one. Different r group properties: charged (+ or -, hydrophobic, hydrophilic, aromatic. Chain of amino acids are linked by peptide bonds: makes a polypeptide. Always same bond no matter the specific amino acid.

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