Evaluating the structural change in adsorbed water in dispersed systems during their hydration by the method of infrared spectroscopy

1981 ◽  
Vol 40 (3) ◽  
pp. 275-280
Author(s):  
P. P. Olodovskii
Keyword(s):  
Infrared Spectroscopy ◽  
Structural Change ◽  
Adsorbed Water ◽  
Dispersed Systems

Real-Time Pursuit of Crystal Growth by Millisecond Time-Resolved Multichannel Fourier Transform Infrared Spectroscopy

1998 ◽  
Vol 52 (2) ◽  
pp. 222-225
Author(s):  
Mamoru Hashimoto ◽  
Hiro-O Hamaguchi
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Structural Change ◽  
Liquid Phase ◽  
Fourier Transform Infrared Spectroscopy ◽  
Molecular Orientation ◽  
Structural Changes ◽  
Fourier Transform Infrared ◽  
Time Resolved ◽  
Recovery Curves

The surface (about 130 molecular layers) of an oriented thin crystal of decanoic acid was subjected to sudden melting by a laser-induced temperature jump (T-jump), and the process of subsequent crystal re-growth was monitored by millisecond time-resolved multichannel Fourier transform infrared spectroscopy. The gauche–trans structural change of the alkane part of the molecule has been probed by the CH stretch bands in the 2800–3000 cm−1 region. The change in the molecular orientation has been detected by the OH stretch band around 3065 cm−1. The recovery curves for the CH2 antisymmetric stretch and the OH stretch bands are markedly different from each other in the first 200 ms, suggesting that the gauche–trans structural changes precedes the crystal re-growth. After 500 ms, the recovery curves become identical. This result means that the rate of the gauche to the trans structural change is equal to the rate of the recovery of the molecular orientation. It is highly likely that a fast equilibrium is attained between the gauche and the trans conformations in the liquid phase after 500 ms from the sudden melting and that the crystal re-growth takes place solely via the all-trans structure in the liquid phase.

Near Infrared Spectroscopy of Aurichalcite (Zn,Cu2+)5(CO3)2(OH)6

2007 ◽  
Vol 15 (2) ◽  
pp. 115-121 ◽  
Author(s):  
B. Jagannadha Reddy ◽  
Ray L. Frost
Keyword(s):  
Infrared Spectroscopy ◽  
Near Infrared Spectroscopy ◽  
Near Infrared ◽  
Divalent Cations ◽  
Spectral Feature ◽  
Adsorbed Water ◽  
Absorption Bands ◽  
Bending Vibrations ◽  
Show Evidence ◽  
Spectroscopy Studies

In this endeavour, near infrared spectroscopy studies show evidence of variable composition in aurichalcite minerals of zinc copper carbonate hydroxides. The observation of a broad feature in the electronic part of the spectrum around 11,500 cm−1 (870 nm) is a strong indication of Cu2+ substitution for Zn2+ in the mineral. Overtones of OH vibrations in the spectra from 7250 to 5400 cm−1 (1380–1850 nm) show strong hydrogen bonding in these carbonates. A band common to spectra of all carbonates appears near 5400 cm−1 (1850 nm) due to the combination of both OH-stretching and HOH-bending vibrations, which may be attributed to adsorbed water. Aurichalcite minerals display a spectral sequence of five absorption bands with variation of both band positions and intensities and this is the chief spectral feature observed in the range 5200–5100 cm−1 (1920–2380 nm) due to vibrational processes of the carbonate ion. The frequency shift of carbonate bands suggests the effect of divalent cations and/or variations of the Zn/Cu ratio in aurichalcite minerals.

scholarly journals Water Structure in Proteins in Solid State Studied by Near Infrared Spectroscopy

2017 ◽  
Vol 735 ◽  
pp. 168-172
Author(s):  
Siraporn Soonthonhut ◽  
Alfred A. Christy
Keyword(s):  
Infrared Spectroscopy ◽  
Near Infrared Spectroscopy ◽  
Water Adsorption ◽  
Near Infrared ◽  
Free Water ◽  
Adsorbed Water ◽  
Water Molecules ◽  
Combination Frequency ◽  
Adsorption Of Water ◽  
Combination Frequencies

Water adsorption in proteins is the crucial process of protein folding and structure stabilizing. Adsorption of water on proteins can be evaluated by near-infrared spectroscopy, a useful technique for observing combination frequency of a water molecule. In this work, albumin, lysozyme, and silk, were used as models for α-helix and β-pleated sheet proteins. Their NIR spectra during water adsorption process were measured by using an NIR spectrometer equipped with a transflectance accessory. Moreover, the quantitative adsorption of water was determined by gravimetric technique. The results indicate that, there are five different NIR absorptions arise from the OH combination frequencies of water adsorbed by albumin in the 5300-5100 cm-1 region. But there are only four absorptions for lysozyme and silk. The OH combination frequencies arising from water molecules in albumin indicate that it acquires free water molecules (5280 cm-1) and adsorbed water molecules through carbonyl-water interactions (5248 and 5160 cm-1) and amino-water interactions (5200 and 5120 cm-1). Interestingly, there is no indication for the presence of free water molecules in lysozyme and silk. Furthermore, the gravimetric results indicate that the rate of water adsorbed follows the order RW.Alb<RW.Lys<RW.Sil and total mass of water adsorbed per gram solid follows the order WAlb<WLys=WSil.

Sign in / Sign up

Export Citation Format

Share Document