1922 L2

Created by suki

why proteins is fundamentals

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Diver functions related to structure 

  • Structural components of cells 

  • Motor proteins 

  • Enzymes 

  • Antibodies 

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why proteins is fundamentals

Diver functions related to structure 

  • Structural components of cells 

  • Motor proteins 

  • Enzymes 

  • Antibodies 

what are the level of strucutre

Primary structure  

  • Peptide bond formation (dehydration reaction) 

  • R groups can be modified --> by giving more energy/ metabolised --> structure changed --> for different functions / purpose (can be positive or negative) 

  • Sequence comparison of multiple homologs of particular protein reveals highly conserved regions that are important for function

  • polar, non-charged amino acis —> dipole, case electrognegativtiy (O/N/S)

  • non-polar amino acids —> H/ alky side chain

Secondary structure  

  • Local folding of residues in regular forms 

  • Alpha helix 

  • Beta sheet  

    • Antiparallel --> terminals reverse  

    • Parallel--> same terminal  

  • Beta turn 

  • Random coil 

Tertiary structure 

  • Global folding of protein chain  

how to determinate structure

X-ray crystallography 

  •  Diffracted by electron --> the more electrons the more diffraction  

  • Electron density map is created --> analyse to find out what kind of atom is it --> help bind the protein structure  

  • The diffraction equation allow to calculate the distance between two atom (bond length) 

  •  Lower the resolution increase the clarity of the structure 

Nuclear magnetic resonance spectroscopy 

  • Odd atomic number or an odd mass number has a nuclear spin  

  • Spinning charge nucleus generated a magnetic field  

  •  Signal is produce by changing the external magnetic field --> spinning direction change  

  • When the spinning nuclei align with the magnetic field --> lower energy more stable 

  • When the spinning nuclei against the magnetic field --> higher energy less stable 

  • The peak (intensity) in the spectroscopy graph show the number of proton in the environment 

  • The magnetic field strength (location of the signals)  provide structure information/ chemical environment  

  • Number of signals show how many different kinds of protons are present  

  • Signal splitting show the number of protons on adjacent atoms  

Electron diffraction +microscopy 

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