Zellbiologie
Cellular bricks I+II
Cellular bricks I+II
Fichier Détails
| Cartes-fiches | 50 |
|---|---|
| Langue | English |
| Catégorie | Biologie |
| Niveau | Université |
| Crée / Actualisé | 01.01.2017 / 05.01.2017 |
| Lien de web |
https://card2brain.ch/box/20170101_zellbiologie1
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amino acid
nonpolar side chains
Amphipathic
(chemistry) describing a molecule, such as a detergent, which has both hydrophobic and hydrophilic groups.
Proteins Functions
Proteins Functions: Enzymes, storage proteins, signal proteins, structural proteins, receptor proteins, transport proteins, motor proteins and gene regulatory proteins.
Proteins Primary structure
Proteins Primary structure: Amino acid sequence --> stabilised only by covalent peptide bonds
Protein Secondary structure:
Protein Secondary structure: Folding of the polypeptide structure (hydrophilic side chains on the outside),
usually as α-helix and/or β-sheet(parallel/antiparallel) --> stabilised by non-covalent bonds such as hydrogen bonds of the
peptide backbone
Proteins Tertiary structure:
Proteins Tertiary structure: Folding of separate elements of the secondary structure --> stabilised by non-
covalent interactions between the side chains of the amino acids and covalent disulphide bonds.
Proteins Quaternary structure:
Proteins Quaternary structure: Assemblies of several subunits to a complex protein --> stabilised by covalent
and non-covalent bonds.
Identical polypeptide chains: homodimers, homooligomers
Different polypeptide chains: heterodimers, heterooligomers
Protein complexes
peptide bond
- resonance between the amide-nitrogen and the carbonyl-oxygen affects that the peptide bond is planar and fixed.
- rotations around the α-carbon atom are possible.
- the side chains at the α-C of neighbouring amino acids determine the flexibility
- protein folding is independent of this flexibility.
Three types of non covalent bonds in proteins
