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Proteins (Amino Acids (Polar (no charge) (Phosphorylation (Serine,…
Proteins
Amino Acids
POSITIVE
Histidine
Arginine
Lysine
NEGATIVE
Aspartate
Glutamate
Polar (no charge)
Cysteine
Insulin Synthesis
Phosphorylation
Serine
Threonine
Asparagine
Glutamine
Non polar
Others
Alanine
Proline
Glycine
Branch Chain
Leucine
Isoleucine
Valine
Sulfur
Containing
Methionine
Aromatic
Phenylalanine
Tyrosine
Tryptophan
Structure
Secondary
Alpha helix
R groups point out
Every carbonyl O H bonds with an amide H 4 residues apart
Beta Sheet
Parallel or antiparallel interchain hydrogen bonds
Sheets have 2-5 strands
Beta Turn
Type 1
Proline
Type 2
Glycine
Tertiary
Chaperone proteins
Protein folding
Refolding
Proteolytic systems
Chaperone mediated autophagy
Macroautophagy
Ubiquitin
Subunit formation
Disorders
Examples
Mad cow
Transthyretin amyloidosis
Alzheimers
Interfere with ECM
Soluble to insoluble proteins
Bonds/Interactions
Covalent
Peptide bond
Peptidyl transferase
Non Covalent
Van der Waals
Hydrogen Bonds
Ionic Bonds
Quaternary
Hemoglobin
Structure
Adult
Fetal
Regulation
H+
Bind oxyhemoglobin
2,3-BPG
Bind DEoxyhemoglobin
CO2
Bind oxyhemoglobin
Disorders
Sickle Cell Anemia
Glutamic acid (charged) to valine (uncharged) point mutation
Thalasemmias
Beta Type
Alpha precipitates out because no beta to interact with
Alpha type
Hydrops fetalis
Collagen
Structure
Triple helix
Two alpha 1
One alpha 2
1000 AA
Proline/Hydroxyproline
Glycine
Defects
Genes
COL1A2
COL1A1
Mutation type
Glycine substitution
Osteogenesis imperfecta
Non functional allele
Reduced amount of collagen