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TLS Online TPP Program

#Id: 611

The answer probably lies in the fact that repression of the trp operon is weak—much weaker.

#Unit 2. Cellular Organization #Trp Operon #Part B Pointers
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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.