Zellbiologie

Cellular bricks I+II

Cellular bricks I+II


C. W.
This flashcard set delves into the intricate world of cellular biology at a university level, focusing on the structure and function of molecules like proteins, acids, and lipids. It explores the bonds that hold these molecules together, the energy they store, and their roles in cellular processes. The set is rich with images to illustrate concepts like the primary, secondary, tertiary, and quaternary structures of proteins, as well as the various types of bonds and their significance. This flashcard set is invaluable for university students studying biology, providing a comprehensive overview of cellular components and their interactions.
Karten
50
Lernende
2
Sprache
Englisch
Kategorie
Biologie
Stufe
Universität
Erstellt / Aktualisiert
01.01.2017 / 05.01.2017

Lernkarten

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

Lernen