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Noncovalent Interactions That Determine the Structure of a Protein Molecule in Water

3 NONCOVALENT INTERACTIONS THAT DETERMINE THE STRUCTURE OF A PROTEIN MOLECULE IN WATER [Pg.235]

Protein folding requires that the large conformational entropy opposing the folded state be outweighed by the sum of the enthalpic and other entropic factors that affect the stability of the folded state. The most important interactions determining the protein structure in water are briefly reviewed in the following sections. [Pg.235]

FIGURE 13.7 Polar and nonpolar contributions made to the water-accessible surface of different proteins. [Pg.236]




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A interactions

A) determinations

Determination of as

Determination of protein

Determination of the Structure

Interaction of molecules

Molecule interaction

Molecules determination

Molecules of water

Molecules structures

Noncovalent

Noncovalent interactions in proteins

Protein noncovalent

Protein water molecules

Protein, determination

Protein-water interactions

Proteins determining

Structural molecules

Structural water

Structure Proteins Water

Structure of proteins

Structure, of a molecule

Structured water

Structures interaction

Structures of molecules

The determined structures

The structure of water

The water molecule

Water determination

Water molecule

Water molecule molecules

Water molecules structures

Water proteins

Water structuring

Water, structure

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