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Protein Structure - Coggle Diagram
Protein Structure
Amino Acids
Types
Polar- Tyrosine, tryptophan, asparagine, glutamine. cytesine, serine, theronine
nonpolar- glycine, alanine, valine, leucine, isoleucine, methionine, phenylalanine
charged- histidine, asparate, glutamine, lysine
Tyrosine, tryptophan and phenylalanine absorb and give uniques UV spectrums
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pH alteration
pKa
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it is protonated when pH is less than pH, since it is surrounded by protons
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Modifications
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modification by phosphorylation, which makes it negative
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Folding
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Levinthal paradox- assume each carbon can have one of three bond angles for 100 amino acids then th etime it takes for the formation of the correct structure is 1.6x10^27 years, so the searching process is not random
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Primary Structure
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it is the linear covalent arrangement if amino acid residues on the and its C-terminal amino acid on the right
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Secondary Structure
Alpha helix
hydrogen bonds
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all H-bonds in same orientation which creates a dipole so N-terminus is positive and C-terminus negative
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Pro (because of bonding of amino group to carbon in side chain prevents stabilising through normal hydrogen bonding) and Gly are unable to form helices
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Beta Sheet
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can curve around and form a cylinder, called a beta barrel
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Quaternary Structure
can be dimers, trimers, tetramers (icosahedral are found in viruses)
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