Hydrogen bond intermolecular force

The term polymer is derived from the Greek words poly and meros, meaning many parts. We noted in the last section that the existence of these parts was acknowledged before the nature of the interaction which held them together was known. Today we realize that ordinary covalent bonds are the intramolecular forces which keep the polymer molecule intact. In addition, the usual type of intermolecular forces—hydrogen bonds, dipole-dipole interactions, and London forces—hold assemblies of these molecules together in the bulk state. The only thing that is remarkable about these molecules is their size, but that feature is remarkable indeed. 

KEY TERMS intermolecular forces hydrogen bonding polymer... 

OH (hydroxyl) group general formula intermolecular forces hydrogen bonding... 

Formula H2O MW 18.015 bent molecule H-O-H bond angle 104.5° H-0 bond distance 0.9575 A bond dissociation energy of 0-H bond 101.2 kcal/mol intermolecular force hydrogen bonding... 

Given the following intermolecular forces— hydrogen bonds, London dispersion forces, ionic interactions and dipole-dipole interactions—if arranged in order from the strongest to the weakest the order would be... 

The technique of noncovalent derivatization employs the noncovalent intermolecular forces (hydrogen bonding, 7t-stacking, UpophUic-lipophilic interactions, and electrostatic interactions) to trap the molecular species in organized matrices. 

Water is an example of a substance with large intermolecular forces (hydrogen bonding). 

In addition to the intramolecular covalent bonds that keep the polymer molecules intact, we now know that intermolecular forces— hydrogen bonds,... 

Charge transfer complexes, molecular addition compounds, weak intermolecular forces, hydrogen bonds... 

PowerLecture Intermolecular Forces Hydrogen Bonding Forces... 

While dissolved protein molecules possess a definite secondary and tertiary structure, denatured proteins are unfolded extensively. Their X-ray diagram resembles the one of 8-keratin, i.e. one of almost straight peptide chains. This structure is firmly held in place by intermolecular forces (hydrogen bonds and salt bonds), which develop randomly. During the reorientation process, at least some of the disulfide bonds (if present) must be ruptured and, in fact, the number of reactive HS groups does grow. Other functional groups of the side chains, e.g. of tyrosine, often become more reactive in denatured proteins. 

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