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TLS Online TPP Program

#Id: 8056


Glu–Cys–Gly peptide in which the γ-carboxylate group of the glutamate side chain forms an isopeptide bond.

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

#Id: 8276

#Unit 1. Structure and Function of Biomolecules

TLS Online TPP Program

#Id: 8277

#Unit 1. Structure and Function of Biomolecules

For maximum stability, the donor pair (AH) and the acceptor (B) are usually colinear (that is, i., AHB = 180°), but deviations of up to 30° are known.

TLS Online TPP Program

#Id: 8278

#Unit 1. Structure and Function of Biomolecules

Plot of density versus temperature for liquid water.
The maximum density of water is reached at 4°C.
The density of ice at 0°C is 0.9167 g cm-3•

TLS Online TPP Program

#Id: 8279

#Unit 1. Structure and Function of Biomolecules

Charge–charge (ionic) interactions
These interactions occur between the side chains of oppositely charged residues as well as between the NH3+ and COO− groups at the ends of polypeptide.

TLS Online TPP Program

#Id: 8280

#Unit 1. Structure and Function of Biomolecules

Coulomb’s law describes the potential energy (V) between two separated charges (in a perfect vacuum) according to the relationship.

TLS Online TPP Program

#Id: 8281

#Unit 1. Structure and Function of Biomolecules

In absence of water the magnitude of the charge–charge interaction is significantly greater.

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