Protein Flashcards
Aromatic amino acids
Tyrosine
Tryptophan
Phenylalanine
Most basic and most acidic protein
Basic - Arginine
Acidic - Aspartate
Amino acid per residues and pitch of alpha helix
3.6 amino acid per residues
Pitch - 0.54nm
Axial rise of alpha and beta protein
1.5 Å and 3.5 Å
Amino acid in Collegen
Glycine, proline and hydroproline/ hydroxylysine
Amino acid helps in hydroxylation of Collegen
Ascorbic acid
Amino acid of Elastin and Keratins
Glycine and Proline
Cysteine
Molecular chaperone and eg.
Proteins that help in interaction with other protein and aid in their folding.
Eg. Foldases and holdases.
Two subcomplex of proteasome
20S core and 19S proteasome forms 26 S or 30 S Proteasome.
Ubiquitin binds to protein by which bond and by which residue.
Covalent bond and by lysine residue
Ring of the following
Phenylalanine
Tryptophan
Cysteine
Histidine
Phenylalanine - Phenyl ring
Tryptophan - Indole ring
Cysteine - Sulfhydryl or thiol group
Histidine - Imidazole ring
Deamination of 5 methyl cytosine
Cytosine
Adenine
Guanine
Thymine
Uracil
Hypoxanthine
Xanthine
Degrons
Aka degradation signal guides the metabolic stability of proteins.
N degron
The first amino acid present in the n terminal that causes degradation
N end rule pathway
Proteins with degrons degrade protein by this pathway by ubiquitination