The role of hydrogen bonds in protein folding and protein association

Journal Article · Thu Feb 07 00:00:00 EST 1991 · Journal of Physical Chemistry; (United States)

DOI:https://doi.org/10.1021/j100156a074· OSTI ID:5266907

Ben-Naim, A ^[1]

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1. National Inst. of Health, Bethesda, MD (USA)

The contribution of a pair of functional groups that can form either intermolecular or intramolecular hydrogen bonds to the total standard free energy of the process of protein folding or protein association is examined. It is found that this contribution can be quite large, either positive or negative, depending on the particular process and on the solvent density. This is in contrast to the common belief that the hydrogen-bond energies tend to be compensated in these processes. For the binding process, in which the two functional groups are completely removed from the aqueous environment, the contribution of such a pair of functional groups to {Delta}G can be as high as +6.4 kcal/mol. This is the main reason why hydrophobic rather than hydrophilic surfaces tend to attach to each other. In contrast, when the two functional groups are only partially removed from the aqueous environment, as in the case of the formation of {alpha}-helix, their contribution to {Delta}G can be negative and of the order of about 1 kcal/mol.

• OSTI ID: 5266907
• Journal Information: Journal of Physical Chemistry; (United States), Vol. 95:3; ISSN 0022-3654
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PROTEIN STRUCTURE
CONFORMATIONAL CHANGES
CALCULATION METHODS
CHEMICAL BONDS
FREE ENTHALPY
MOLECULAR STRUCTURE
THEORETICAL DATA
DATA
ENERGY
INFORMATION
NUMERICAL DATA
PHYSICAL PROPERTIES
THERMODYNAMIC PROPERTIES
550200* - Biochemistry