tc:aatet.ti i . / i l i z a f i o i i Rrxearch 42 Ilevelopnietct Ilivisioti , I J . W A , ' 4 RS ~ l'hilatlelphia, Peritisylvan?a 1.91 I8 SynopsisThe iiifrared spectra of uiideiiatured bovine teiidoii ~~l l a g e i i were iiivestigated a t 25°C :tiid relative hiimidities from 0 to 95%. Suitable samples were prepared by forcing froaeii suspensioiis of the material in distilled water through a stainless steel capillary. The samples were investigated by electron microscopy before and after the spectra were obtained to asrertaiii that no denaturation had taken place while the sample was exposed t o infrared radiatioii. Temperature controlled absorptioii cells were constructed which permitted the passing of sir with a kiiowii water content over t,he sample film. Gradual changes were observed in the freyiieiicies arid iiiteiisities of characteristic amide bands civer the relative huniidity raiige of 0 to 75Yc. These changes are particularly proiioiuived for the amide I1 band, associated with beiidiiig motions of peptide N H bonds. They lend to the c:oiicliisioii that water molecules are gradually attached to peptide NH bonds within the triple helix over a aide rniige of relative humidity. Changes in CH deformation haiids suggest that CH to 0 hydrogen bonding does occur and that it is more pronoiiriced i i i rollngeii exposed t o high i,elative hiirnidity. 0 1!)71 I)y Jotiii Wiley ti S(iii,, Iiir. SOC., 25,173 (1958).

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