TLS Online TPP Program

#Id: 360


The cytosolic isozymes has two distinct function, It catalyzes the conversion of citrate to isocitrate, providing the substrate for a cytosolic isocitrate dehydrogenase that generates NADPH as reducing power for fatty acid synthesis and other anabolic processes in the cytosol. It also has a role in cellular iron homeostasis

#Unit 1. Structure and Function of Biomolecules #atom #Part B Pointers
More Pointers
TLS Online TPP Program

#Id: 8754

#Unit 1. Structure and Function of Biomolecules

The mammalian protein p53 also have both structured and unstructured segments. With its unstructured region at the carboxyl terminus four different proteins.

TLS Online TPP Program

#Id: 8755

#Unit 1. Structure and Function of Biomolecules

Thermodynamic measurements indicate that native proteins are only marginally stable under physiological conditions. The free energy required to denature them is ∼0.4 kJ ∙ mol−1 per amino acid residue.

TLS Online TPP Program

#Id: 8756

#Unit 1. Structure and Function of Biomolecules

Protein stability is the net balance of forces, which determine whether a protein will be in its native folded conformation or a denatured state.

TLS Online TPP Program

#Id: 8757

#Unit 1. Structure and Function of Biomolecules

A fully folded 100-residue protein is only about 40 kJ ∙ mol−1 more stable than its unfolded form (for comparison, the energy required to break a typical hydrogen bond is ∼20 kJ ∙ mol−1).

TLS Online TPP Program

#Id: 8758

#Unit 1. Structure and Function of Biomolecules

The combined hydrophobic and hydrophilic tendencies of individual amino acid residues in proteins can be expressed as hydropathies. The greater a side chain’s hydropathy, the more likely it is to occupy the interior of a protein.

TLS Online TPP Program

#Id: 8759

#Unit 1. Structure and Function of Biomolecules

Hydrogen bonds, which are central features of protein structures, make only minor contributions to protein stability.