Time-resolved Fourier Transform Infrared Spectroscopy Research Articles

Time-Resolved FDTD and Experimental FTIR Study of Gold Micropatch Arrays for Wavelength-Selective Mid-Infrared Optical Coupling.

Infrared radiation reflection and transmission of a single layer of gold micropatch two-dimensional arrays, of patch length ∼m and width ∼m, have been carefully studied by a finite-difference time-domain (FDTD) method, and Fourier-transform infrared spectroscopy (FTIR). Through precision design of the micropatch array structure geometry, we achieve a significantly enhanced reflectance (85%), a substantial diffraction (10%), and a much reduced transmittance (5%) for an array of only 15% surface metal coverage. This results in an efficient far-field optical coupling with promising practical implications for efficient mid-infrared photodetectors. Most importantly we find that the propagating electromagnetic fields are transiently concentrated around the gold micropatch array in a time duration of tens of ns, providing us with a novel efficient near-field optical coupling.

Thermal decomposition kinetics and mechanism of low-temperature hydrogenated acrylonitrile butadiene rubber composites with sodium methacrylate

Thermal decomposition processes and mechanism of low-temperature grade hydrogenated acrylonitrile butadiene rubber(LTG-HNBR) composites with sodium methacrylate(NaMAA) were investigated by thermogravimetric analysis(TGA) and Fourier transform infrared spectroscopy(FTIR) coupling technology in this article. The results of TGA demonstrate that the addition of NaMAA can enhance the thermal decomposition temperature of the rubber. Moreover, it was found that the composites spent more activation energies to decompose than pure rubber by the calculations of multiply heating rate method. Time-resolved FTIR spectra show that NaMAA affects the initial decomposition of the composites. But in the following process, the composites maintained a similar behavior to the matrix. During the decomposition, PNaMAA nanostructures, in-situ generated by NaMAA, helped reduce the diffusion speed of decomposition products and thus improved the thermal stability of the composites. We believe that these findings can provide some guides to direct the applications of LTG-HNBR composites with unsaturated metal methacrylates.

Conformation Transitions of Recombinant Spidroins via Integration of Time-Resolved FTIR Spectroscopy and Molecular Dynamic Simulation.

Current trends in biomaterial designs require a detailed understanding of structure-function relationships to efficiently address specific utilities. As a prototype, spider silk has been widely studied with diversified characterization or simulation methods, exploiting the integration of experimental and modeling approaches to gain insight into structure-function relationships. However, the assembly mechanisms of spider silk in natural and non-natural environments remain incompletely understood. In the present study, experimental and simulation approaches were utilized to study assembly mechanisms of recombinant spider silks. Two spider silk constructs, H(AB)12 and H(AB)12NtSp, were produced and studied. Deconvoluted Fourier transform infrared spectroscopy (FTIR) spectra and molecular dynamics simulations, before and after ethanol treatment, were analyzed to quantify secondary structures, and a higher helix content was observed in H(AB)12NtSp compared with that in H(AB)12. Time-resolved FTIR analysis was used to monitor conformation transitions. A higher rate of β-sheet formation was found in H(AB)12NtSp compared with that in H(AB)12. These results suggest that the N-terminal domain accelerates self-assembly of recombinant spidroins under ethanol treatment. The approaches used in this study provide insights into the function of the N-terminal domain in conformational transitions of spider silks under non-natural conditions as well as fiber formation. This approach should enable more efficient design, synthesis, and preparation of new recombinant spidroin materials with tunable mechanical properties.

Synthesis of mesoporous titania–graphite composite templated by hypocrellins for visible-light photocatalytic degradation of acetaldehyde

A photoactive compound extracted from a fungus (Hypocrella bambuase), named hypocrellins, was used as template to synthesize thermally stable mesoporous materials. The synthesized mesoporous titania samples were characterized using a combination of various physicochemical techniques, such as N2 adsorption/desorption measurement, X-ray diffraction (XRD), scanning electron microscopy (SEM), transmission electron microscopy (TEM), X-ray photoelectron spectroscopy (XPS), UV–vis diffuse reflectance spectroscopy (DRS) and Fourier transform infrared spectroscopy (FT-IR). The results of physicochemical characterizations showed that the as-synthesized sample was a composite of highly crystalline mesoporous anatase titania and graphitic carbon (gc–MTiO2), which implies the dual function of hypocrellins as template and “dopant”. The in situ doped graphitic carbon significantly increased the visible-light absorbance of TiO2. The gc–MTiO2 exhibited efficient photocatalytic activity under visible-light for photodegradation of acetaldehyde, a common indoor air pollutant. The photophysics and electron dynamics in this photocatalytic process were studied by time-resolved FT-IR spectra, in particular on the nano- to milli-second time scale. It is observed that electrons were injected into the conduction band of gc–MTiO2 and they were decayed to deep traps caused by graphitic carbon. The reported strategies could open up new uses for mesoporous titania self-doped with carbon in applications such as solar cells, photocatalysts, photoelectrical devices, and photo-induced sensors.

Effect of methylcellulose on the formation and drug release behavior of silk fibroin hydrogel

In this study, methylcellulose (MC) was used to control the gelation time of silk fibroin (SF) aqueous solution. The gelation time was measured using a Vibro Viscometer at 50°C. Fourier transform infrared spectroscopy (FT-IR), scanning electron microscopy (SEM), and a texture meter were used to investigate the effect of MC on the hydrogelation of SF solution. SF/MC hydrogels could be formed by the addition of MC, although their gelation time was increased with MC content. To examine the conformational change of SF/MC hydrogels, time-resolved FT-IR spectra were obtained at constant temperature using a custom-made IR chamber. From FT-IR spectra focused on the amide I peak position, the transition of SF molecules in SF/MC solution from a random coil to a β-sheet structure was inhibited in the presence of MC molecules. In addition, the drug release of SF/MC hydrogels loaded with 5-aminosalicylic acid was studied in 2-dimensional (2-D) and 3-dimensional (3-D) conditions in vitro. The drug release behavior of SF or SF/MC hydrogels was measured using UV–Vis spectroscopy. The release rate of 5-aminosalicylic acid in SF/MC hydrogel was lower than that of SF hydrogel, which may be closely associated with the hydrophilic interaction between MC and 5-aminosalicylic acid. This approach to controlling the sol–gel transition and the drug release of SF hydrogels by the addition of MC will be useful in the design and tailoring of novel materials for biomedical applications.

Spectroscopic and Kinetic Investigation of the Fully Reduced and Mixed Valence States of ba3-Cytochrome c Oxidase from Thermus thermophilus

The complete understanding of a molecular mechanism of action requires the thermodynamic and kinetic characterization of different states and intermediates. Cytochrome c oxidase reduces O(2) to H(2)O, a reaction coupled to proton translocation across the membrane. Therefore, it is necessary to undertake a thorough characterization of the reduced form of the enzyme and the determination of the electron transfer processes and pathways between the redox-active centers. In this study Fourier transform infrared (FTIR) and time-resolved step-scan FTIR spectroscopy have been applied to study the fully reduced and mixed valence states of cytochrome ba(3) from Thermus thermophilus. We used as probe carbon monoxide (CO) to characterize both thermodynamically and kinetically the cytochrome ba(3)-CO complex in the 5.25-10.10 pH/pD range and to study the reverse intramolecular electron transfer initiated by the photolysis of CO in the two-electron reduced form. The time-resolved step-scan FTIR data revealed no pH/pD dependence in both the decay of the transient Cu(B)(1+)-CO complex and rebinding to heme a(3) rates, suggesting that no structural change takes place in the vicinity of the binuclear center. Surprisingly, photodissociation of CO from the mixed valence form of the enzyme does not lead to reverse electron transfer from the reduced heme a(3) to the oxidized low-spin heme b, as observed in all the other aa(3) and bo(3) oxidases previously examined. The heme b-heme a(3) electron transfer is guaranteed, and therefore, there is no need for structural rearrangements and complex synchronized cooperativities. Comparison among the available structures of ba(3)- and aa(3)-cytochrome c oxidases identifies possible active pathways involved in the electron transfer processes and key structural elements that contribute to the different behavior observed in cytochrome ba(3).

Time-resolved FTIR spectroscopy for monitoring protein dynamics exemplified by functional studies of Ras protein bound to a lipid bilayer

Time-resolved Fourier transform infrared (FTIR) difference spectroscopy is a valuable tool for monitoring the dynamics of protein reactions and interactions. Absorbance changes can be monitored with time resolutions down to nanoseconds and followed for time periods that range over nine orders of magnitude. Membrane proteins bound to solid supported lipid bilayers can be investigated in near physiological conditions with the attenuated total reflection (ATR) technique. Here, we review the basics of time-resolved FTIR with a focus on Ras, a GTPase that is mutated in 25% of human tumors. We show the first time-resolved measurements of membrane anchored Ras and observed the switching between its activated and its inactivated state. We compared those measurements with measurements of the truncated Ras in solution. We found that both the kinetics and the functional groups involved were very similar. This suggested that the membrane did not have a major influence on the hydrolysis reaction.

ChemInform Abstract: Time‐Resolved FT‐IR Spectroscopy of Membrane Proteins

AbstractReview: 66 refs.

Time-resolved FT-IR Spectroscopy of Membrane Proteins

Time-resolved Fourier transform infrared spectroscopy (FT-IR) offers distinct advantages concerning restrictions pertinent to biomolecules. In particular, it is possible to monitor the temporal evolution of the reaction mechanism of complex machineries as membrane proteins, where other techniques encounter significant experimental difficulties. Here, we present the classical principles and experimental realizations of time-resolved FT-IR spectroscopy together with recent developments employed in our laboratory. Examples from applications to retinal proteins are reviewed that underline the impact of time-resolved FT-IR spectroscopy on the understanding of protein reactions on the level of single bonds.

Histidine is involved in coupling proton uptake to electron transfer in photosynthetic proteins

In photosynthesis, the central step in transforming light energy into chemical energy is the coupling of light-induced electron transfer to proton uptake and release. Despite intense investigations of different photosynthetic protein complexes, including the photosystem II (PS II) in plants and the reaction center (RC) in bacteria, the molecular details of this fundamental process remain incompletely understood. In the RC of Rhodobacter (Rb.) sphaeroides, fast formation of the charge separated state, P +Q A −, is followed by a slower electron transfer from the primary acceptor, Q A, to the secondary acceptor, Q B, and the uptake of a proton from the cytoplasm. The proton transfer to Q B takes place via a protonated water chain. Mutation of the amino acid AspL210 to Asn (L210DN mutant) near the entry of the proton pathway can disturb this water chain and consequently slow down proton uptake. Time-resolved step-scan Fourier transform infrared (FTIR) measurements revealed an intermediate X in the Q A −Q B to Q AQ B − transition. The nature of this transition remains a matter of debate. In this study, we investigated the role of the iron–histidine complex located between Q A and Q B. We used time-resolved fast-scan FTIR spectroscopy to characterize the Rb. sphaeroides L210DN RC mutant marked with isotopically labeled histidine. FTIR marker bands of the intermediate X between 1120 cm −1 and 1050 cm −1 are assigned to histidine vibrations and indicate the protonation of a histidine, most likely HisL190, during the disappearance of the intermediate. Based on these results we propose a novel mechanism of the coupling of electron and proton transfer in photosynthesis.

Label-Free Screening of Drug—Protein Interactions by Time-Resolved Fourier Transform Infrared Spectroscopic Assays Exemplified by Ras Interactions

Time-resolved Fourier transform infrared (FT-IR) spectroscopy can reveal molecular details of protein interactions. Analysis of difference spectra selects the absorptions of respective protein groups involved in an interaction against the background of the whole sample. By comparison of the same difference spectrum with and without a small molecule, one can determine whether the small molecule interferes with the protein or not. Usually a marker band of a specific residue of the protein is monitored. Here, we show three different time-resolved FT-IR assays detecting interactions of potential small molecules for molecular therapy with the GTPase Ras as an example for small GTPase binding proteins. Ras regulates signal transduction processes through a switching mechanism, cycling between an active "on" GTP-bound form and an inactive "off" GDP-bound state. Molecular defects in Ras can impair the ability of Ras and the Ras-RasGAP complex to hydrolyze GTP, contributing to uncontrolled cell growth and cancer. Oncogenic mutated Ras is found in about 30% of all cancer cells. We show in vitro assays, indicating (I) the shift of Ras into its "off" conformation, which inhibits the Ras pathway; (II) down-regulation of Ras signaling by changes in the Ras-Raf effector interaction; and (III) down-regulation of Ras signaling pathway by catalyzing GTP hydrolysis. Since almost all molecules have characteristic marker bands in the infrared, time-resolved FT-IR spectroscopy can be used label-free. No artificial nucleotides that could influence the interaction are needed. Both, sample preparation and evaluation can be automated in order to allow for high-throughput screening.

Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins

The introduction of time-resolved Fourier transform infrared (FT-IR) spectroscopy to biochemistry opened the possibility of monitoring the catalytic mechanism of proteins along their reaction pathways. The infrared approach is very fruitful, particularly in the application to membrane proteins where NMR and X-ray crystallography are challenged by the size and protein hydrophobicity, as well as by their limited time-resolution. Here, we summarize the principles and experimental realizations of time-resolved FT-IR spectroscopy developed in our group and compare with aspects emerging from other laboratories. Examples of applications to retinal proteins and energy transduction complexes are reviewed, which emphasize the impact of time-resolved FT-IR spectroscopy on the understanding of protein reactions on the level of single bonds.

Time-Resolved Fourier Transform Infrared Spectroscopy of Chemical Reactions in Solution Using a Focal Plane Array Detector

A Fourier transform infrared (FT-IR) microscope equipped with a single as well as a 64 x 64 element focal plane array MCT detector was used to measure chemical reaction taking place in a microstructured flow cell designed for time-resolved FT-IR spectroscopy. The flow cell allows transmission measurements through aqueous solutions and incorporates a microstructured mixing unit. This unit achieves lamination of the two input streams with a cross-section of 300 x 5 microm each, resulting in fast diffusion-controlled mixing of the two input streams. Microscopic measurement at defined positions along the outlet channel allows time-resolved information of the reaction taking place in the flow cell to be obtained. In this paper we show experimental results on the model reaction between formaldehyde and sulfite. Using the single-point MCT detector, high-quality FT-IR spectra could be obtained from a spot size of 80 x 200 microm whereas the FPA detector allowed recording light from an area of 260 x 260 microm focused on its 64 x 64 detector elements. Therefore, more closely spaced features could be discerned at the expense of a significantly lower signal-to-noise (S/N) ratio per spectrum. Multivariate curve resolution-alternating least squares was used to extract concentration profiles of the reacting species along the outlet channel axis.

Time-Resolved Microspectroscopy on a Single Crystal of Bacteriorhodopsin Reveals Lattice-Induced Differences in the Photocycle Kinetics

The determination of the intermediate state structures of the bacteriorhodopsin photocycle has lead to an unprecedented level of understanding of the catalytic process exerted by a membrane protein. However, the crystallographic structures of the intermediate states are only relevant if the working cycle is not impaired by the crystal lattice. Therefore, we applied visible and Fourier transform infrared spectroscopy (FTIR) microspectroscopy with microsecond time resolution to compare the photoreaction of a single bacteriorhodopsin crystal to that of bacteriorhodopsin residing in the native purple membrane. The analysis of the FTIR difference spectra of the resolved intermediate states reveals great similarity in structural changes taking place in the crystal and in PM. However, the kinetics of the photocycle are significantly altered in the three-dimensional crystal as compared to PM. Strikingly, the L state decay is accelerated in the crystal, whereas the M decay is delayed. The physical origin of this deviation and the implications for trapping of intermediate states are discussed. As a methodological advance, time-resolved step-scan FTIR spectroscopy on a single protein crystal is demonstrated for the first time which may be used in the future to gauge the functionality of other crystallized proteins with the molecular resolution of vibrational spectroscopy.

Strain-induced reorientation and mobility in nematic liquid-crystalline elastomers as studied by time-resolved FTIR spectroscopy

Polarized Fourier transform infrared (FTIR) spectroscopy is employed to study the segmental orientation and mobility of liquid-crystalline elastomers (LCEs) with a monodomain structure in response to external mechanical fields parallel and perpendicular to the initial nematic director. The mean orientation and the molecular order parameter of the different molecular moieties referring to the mesogen, the spacer and the network are analyzed in detail. Parallel stretch leaves the mean orientation of the different molecular moieties and its molecular order parameter nearly uninfluenced. Perpendicular stretch results in a threshold-like dependence: for elongation ratios lambda < or = lambda(c) = 1.3 (10 mol% crosslinker density), respectively lambda < or = lambda(c) = 1.6 (5 mol% crosslinker density) no change of the mean orientation and the molecular order parameters is observed, while for lambda > or = lambda(c) all molecular units reorient and their molecular order parameters are strongly decreased. The present studies give no indications that the reorientational dynamics of the network and the mesogens differ as long as the elongation ratio is smaller than lambda(c).

Generation and Characterization of the Selenocysteinyl Radical: Direct Evidence from Time-Resolved UV/Vis, Electron Paramagnetic Resonance, and Fourier Transform Infrared Spectroscopy

The selenocysteinyl radical 1 has been generated for the first time by laser flash photolysis (lambda(exc) = 266 nm) of dimethyl bis(N-tert-butoxycarbonyl)-l-selenocystine 2 and of [(9-fluorenylideneamino)oxycarbonyl]methyl(N-tert-butoxycarbonyl)-l-selenocysteine 3 in acetonitrile and characterized by time-resolved (TR) UV/Vis, Fourier transform infrared (FTIR), and electron paramagnetic spectroscopy in combination with theoretical methods. A detailed product study was conducted using gas chromatography and one- and two-dimensional NMR spectroscopy. In the case of [(9-fluorenylideneamino)oxycarbonyl]methyl(N-tert-butoxycarbonyl)-l-selenocysteine 3, the (9-fluorenylideneamino)oxycarbonyl moiety serves as a photolabile protection group providing a "caged selenocysteinyl radical" suitable for biophysical applications. Cleavage of the diselenide bridge or the selenium-carbonyl bond by irradiation is possible in high quantum yields. Because of the lack of a good IR chromophore in the mid-IR region, the selenocysteinyl radical 1 cannot be monitored directly by TR FTIR spectroscopy. TR UV/Vis spectroscopy revealed the formation of the selenocysteinyl radical 1 from both precursors. The selenocysteinyl radical 1 has a lifetime tau approximately 63 mus and exhibits a strong band located at lambda(max) = 335 nm. Calculated UV absorptions of the selenocysteinyl radical (UB3LYP/6-311G(d,p)) are in good agreement with the experimental results. The use of TR UV/Vis spectroscopy permitted the determination of the decay rates of the selenocysteinyl radical in the presence of two quenchers. The product studies demonstrated the reversible photoreaction of dimethyl bis(N-tert-butoxycarbonyl)-l-selenocystine 2. Products of the photolysis of the "caged selenocysteinyl radical" precursor 3 are dimethyl bis(N-tert-butoxycarbonyl)-l-selenocystine 2, carbon dioxide, and some further smaller fragments. In addition, the photodecomposition of the (9-fluorenylideneamino)oxycarbonyl moiety produced 9-fluorenone-oxime 4, 9-fluoren-imine 5, and 6 and 7 as products of the dimerization of two 9-fluorenoneiminoxy radicals 8.

Product State Distributions of Vibrationally Excited CO(v) for the CH(X2Π) and CH(A2Δ) Channels of the C2H + O(3P) Reaction

The C2H + O(3P) reaction is investigated using time-resolved Fourier transform infrared spectroscopy (TR-FTIR). The C2H and O radicals are produced by 193-nm photolysis of C2H2 and SO2 precursors. Multiple vibrationally excited products are observed from several resulting reaction processes, including products: CO, CO2, C4H2, and CH. For this choice of photolytic precursors, it is observed that the C2H + SO2, C2H2 + O, and the HCCO + O reactions contribute to the observed product signals. To evaluate the contribution of the C2H + SO2 reaction to the removal kinetics of C2H in the C2H2/SO2 system, the room-temperature rate constant for the C2H + SO2 reaction is experimentally determined to be k = (1.1 ± 0.3) × 10-11 cm3 molecule-1 s-1. The time dependencies of the CO and CO2 species are measured experimentally and simulated to determine conditions under which contributions from the several processes that give the same product can be differentiated. Analysis of the nascent vibrational distribution of the CO products from C2H + O suggests the participation of both CH(A2Δ) and CH(X2Π) products, in the ratio of ∼3:2. The surprisal parameters for the vibrational distribution of the CO products of these two channels are found to be −1.5 ± 0.2 and −1.1 ± 0.2, respectively. It is suggested that the reaction proceeds through the HCCO⧧ intermediate, in agreement with earlier studies, but the CH(A2Δ)/CH(X2Π) branching fraction may be larger than previously reported.

Effects of Surface Morphology on the Anchoring and Electrooptical Dynamics of Confined Nanoscale Liquid Crystalline Films

The orientation and dynamics of two 40-nm thick films of 4-n-pentyl-4'-cyanobiphenyl (5CB), a nematic liquid crystal, have been studied using step-scan Fourier transform infrared spectroscopy (FTIR). The films are confined in nanocavities bounded by an interdigitated electrode array (IDA) patterned on a zinc selenide (ZnSe) substrate. The effects of the ZnSe surface morphology (specifically, two variations of nanometer-scale corrugations obtained by mechanical polishing) on the initial ordering and reorientation dynamics of the electric-field-induced Freedericksz transition are presented here. The interaction of the 5CB with ZnSe surfaces bearing a spicular corrugation induces a homeotropic (surface normal) alignment of the film confined in the cavity. Alternately, when ZnSe is polished to generate fine grooves along the surface, a planar alignment is promoted in the liquid crystalline film. Time-resolved FTIR studies that enable the direct measurement of the rate constants for the electric-field-induced orientation and thermal relaxation reveal that the dynamic transitions of the two film structures are significantly different. These measurements quantitatively demonstrate the strong effects of surface morphology on the anchoring, order, and dynamics of liquid crystalline thin films.

Proteorhodopsin is a Light-driven Proton Pump with Variable Vectoriality

Proteorhodopsin, a homologue of archaeal bacteriorhodopsin (BR), belongs to a newly identified family of retinal proteins from marine bacteria, which could play an important role in the energy balance of the biosphere. We cloned the cDNA sequence of proteorhodopsin by chemical gene synthesis, expressed the protein in Escherichia coli cells, purified and reconstituted the protein in its functional active state. The photocycle characteristics were determined by time-resolved absorption and Fourier transform infrared (FT-IR) spectroscopy. The pH-dependence of the absorption spectrum indicates that the p K a of the primary acceptor of the Schiff base proton (Asp97) is 7.68. Generally, the photocycle of proteorhodopsin is similar to that of BR, although an L-like photocycle intermediate was not detectable. Whereas at pH>7 an M-like intermediate is formed upon illumination, at pH 5 no M-like intermediate could be detected. As the photocycle kinetics do not change between the acidic and alkaline state of proteorhodopsin, the only difference between these two forms is the protonation status of Asp97. This is corroborated by time-resolved FT-IR spectroscopy, which demonstrates that proton transfer from the retinal Schiff base to Asp97 is observed at alkaline pH, but the other vibrational changes are essentially pH-independent. After reconstitution into proteoliposomes, light-induced proton currents of proteorhodopsin were measured in a compound membrane system where proteoliposomes were adsorbed to planar lipid bilayers. Our results show that proteorhodopsin is a light-driven proton pump with characteristics similar to those of BR at alkaline pH. However, at acidic pH, the direction of proton pumping is inverted. Complementary experiments were carried out on proteorhodopsin expressed heterologously in Xenopus laevis oocytes under voltage clamp conditions. The following results were obtained. (1) At alkaline pH, proteorhodopsin mediates outwardly directed proton pumping like BR. (2) The direction of proton pumping can be inverted, when Asp97 is protonated. (3) The current can be inverted by changes of the polarity of the applied voltage. (4) The light intensity-dependence of the photocurrents leads to the conclusion that the alkaline form of proteorhodopsin shows efficient proton pumping after sequential excitation by two photons.

Crystallization behavior of DSPE in dimethyl sulfoxide by time-resolved infrared spectroscopy and differential scanning calorimetry

Phase behavior of distearoylphosphatidylethanolamine (DSPE) dispersed in excess dimethyl sulfoxide has been examined by differential scanning calorimetry (DSC) and time-resolved Fourier-transform infrared spectroscopy (FT-IR). Transformation from lamellar-crystalline to liquid-crystalline phase was found to take place at temperature near 94°C upon initial heating and transformation from liquid-crystalline to lamellar-gel phase took place near 81°C during cooling scans. The kinetics of the transformation from liquid crystalline phase to lamellar-gel phase were analyzed by the well-known Avrami equation. The apparent Avrami exponents were found to be about 3 by DSC and time-resolved FT-IR. The effective dimensionality of the growth pattern can then be set as 2.