Hydrogen bonding and stabilization

It should be appreciated that amino acids such as serine, threonine, tyrosine, and cysteine all contain side-chain alcohol or thiol groups that may participate in hydrogen bonding and stabilize a particular protein conformation. 

Hydrogen bonding can occur when the N—H group of one ammo acid unit and the C=0 group of another are close m space conformations that maximize the number of these hydrogen bonds are stabilized by them... 

The three-dimensional conformation of a protein is called its tertiary structure. An a-helix can be either twisted, folded, or folded and twisted into a definite geometric pattern. These structures are stabilized by dispersion forces, hydrogen bonding, and other intermo-lecular forces. 

Likewise, synthetic 2//-azepines isomerize to 3//-azepines in refluxing chloroform (2-3 h) or in tert-butyl methyl ether at room temperature.291 The isomers can be readily separated by chromatography on silica gel, as the more basic 2//-azepines30 have lower Rf values. In contrast, 7-butyl-2//-azepin-2-acetic acid (11), obtained by heating the tert-butyl ester 10 with iodotrimethylsilane, is stabilized by intramolecular hydrogen bonding and shows no tendency to rearrange to the 3//-isomer.291... 

Fig. 14.—Antiparallel packing arrangement of extended, 4-fold, 2,3,6-tri-O-ethylamylose (12) helices, (a) Stereo view of two unit cells approximately normal to the lie-plane. The helix at the center (filled bonds) is antiparallel to the two helices (open bonds) at the comers in the back. There is no intra- or inter-chain hydrogen bond, and only van der Waals forces stabilize the helices, (b) A e-axis projection of the unit cell shows that the ethyl groups extend into the medium in radial directions. 

Fig. 37.—(a) Stereo view of one turn of the 3-fold double helix of welan (43). The two chains are drawn in open and filled bonds for distinction. The vertical line represents the helix axis. Both intra-and inter-chain hydrogen bonds and side chains, hydrogen bonded to carboxylate groups, stabilize the double helix. Calcium ions (crossed circles) are present near the carboxylate groups, but outside the helix to make inter double-helical connections. 

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