Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PROPANEDIOLS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 595 records · Page 33Linked to original sources
PubMed1996

In vitro analysis of the interactions between the PocR regulatory protein and the promoter region of the cobalamin biosynthetic (cob) operon of Salmonella typhimurium LT2.

The PocR protein of Salmonella typhimurium LT2 was overexpressed and used to demonstrate in vitro that it specifically binds to the cobalamin biosynthetic operon (cob) promoter region. Evidence is presented to show that PocR DNA-binding activity in vitro is regulated by the effector molecule 1,2-propanediol. Deletion analysis of the cob promoter (Pcob) suggested that two regions upstream of the promoter are needed for optimal activation of Pcob by PocR in vivo. DNase I footprinting experiments demonstrated that PocR binds to two sites within Pcob. The transcription initiation site of cob mRNA in response to 1,2-propanediol was identified and shown to be different from the one reported for transcription initiation under anoxic conditions in the absence of 1,2-propanediol.

Bacterial Proteins↗
PubMed1997

Repression of the cob operon of Salmonella typhimurium by adenosylcobalamin is influenced by mutations in the pdu operon.

The cob operon encodes functions needed for the biosynthesis of adenosylcobalamin (Ado-B12). Propanediol induces transcription of the cob operon and the neighboring pdu operon, which encodes proteins for the B12-dependent degradation of propanediol. Expression of the cob (but not the pdu) operon is repressed by exogenous cyanocobalamin. Evidence is provided that cob operon repression is signaled by internally generated Ado-B12, which can be formed either by the CobA adenosyltransferase or by an alternative adenosyltransferase (AdoT) that we infer is encoded within the pdu operon. Repression is also affected by mutations (AdoB) in the pdu operon that map upstream of the inferred pdu adenosyltransferase gene. Such mutations allow cobalamin to mediate repression at concentrations 100-fold lower than those needed in the wild type. It is proposed that these mutations eliminate a component of the propanediol dehydratase enzyme complex (PduCDE) and that this complex competes with the cob regulatory mechanism for a limited supply of Ado-B12.

Alkyl and Aryl Transferases↗
PubMed2001

Regulation of carbon and electron flow in Clostridium butyricum VPI 3266 grown on glucose-glycerol mixtures.

The metabolism of Clostridium butyricum was manipulated at pH 6.5 and in phosphate-limited chemostat culture by changing the overall degree of reduction of the substrate using mixtures of glucose and glycerol. Cultures grown on glucose alone produced only acids (acetate, butyrate, and lactate) and a high level of hydrogen. In contrast, when glycerol was metabolized, 1,3-propanediol became the major product, the specific rate of acid formation decreased, and a low level of hydrogen was observed. Glycerol consumption was associated with the induction of (i) a glycerol dehydrogenase and a dihydroxyacetone kinase feeding glycerol into the central metabolism and (ii) an oxygen-sensitive glycerol dehydratase and an NAD-dependent 1,3-propanediol dehydrogenase involved in propanediol formation. The redirection of the electron flow from hydrogen to NADH formation was associated with a sharp decrease in the in vitro hydrogenase activity and the acetyl coenzyme A (CoA)/free CoA ratio that allows the NADH-ferredoxin oxidoreductase bidirectional enzyme to operate so as to reduce NAD in this culture. The decrease in acetate and butyrate formation was not explained by changes in the concentration of phosphotransacylases and acetate and butyrate kinases but by changes in in vivo substrate concentrations, as reflected by the sharp decrease in the acetyl-CoA/free CoA and butyryl-CoA/free CoA ratios and the sharp increase in the ATP/ADP ratio in the culture grown with glucose and glycerol compared with that in the culture grown with glucose alone. As previously reported for Clostridium acetobutylicum (L. Girbal, I. Vasconcelos, and P. Soucaille, J. Bacteriol. 176:6146-6147, 1994), the transmembrane pH of C. butyricum is inverted (more acidic inside) when the in vivo activity of hydrogenase is decreased (cultures grown on glucose-glycerol mixture). For both cultures, the stoichiometry of the H(+) ATPase was shown to remain constant and equal to 3 protons exported per molecule of ATP consumed.

Carbon↗
PubMed1979

Neuropharmacology of sedatives and anxiolytics.

Sedative drugs are intended to cause various degrees of drowsiness. Animal experiments indicate that barbiturates induce these effects primarily by depression of the reticular activating system in the rostral brainstem. This in turn potentiates the thalamic recruiting system, thereby inducing 'barbiturate bursts' in the EEG. Anxiolytic drugs are intended to reduce anxiety or tension at doses which do not cause sedation or sleep. Propanediols may depress deactivating centers in the caudal brainstem, thereby releasing the activating centers in the rostral brainstem and depressing the thalamic recruiting response. These drugs may also act on the amygdala. Benzodiazepines have depressant effects on the amydala or hippocampus. These effects may release the reticular formation from inhibition. Enhanced activity of the activating and deactivating centers, to a different extent in different animals, would produce restlessness in some animals and sedation in others, accompanied by a mixture of fast and slow waves in the EEG. Sedative and anxiolytic agents also have central relaxant effects. The barbiturates act directly on the spinal cord, depressing both monosynaptic and polysynaptic reflexes. Propanediols and benzodiazepines act primarily on the descending facilitatory influence of the brainstem. Reduction of this influence depresses spinal polysynaptic but not monosynaptic reflexes. Biochemical studies suggest that barbiturates may act by antagonizing synaptic excitation induced by glutamate. Benzodiazepines may act by enhancing presynaptic inhibition mediated by GABA. The mechanism of action of propanediols is unknown.

Animals↗
PubMed1992

Vitrification of bovine blastocysts obtained by in vitro culture of oocytes matured and fertilized in vitro.

Two experiments were conducted to assess the viability of bovine blastocysts obtained by in vitro fertilization of oocytes matured in vitro (IVM-IVF) and cryopreserved by vitrification. In Expt 1, the optimal concentrations of glycerol and 1,2-propanediol in the basic medium (modified TCM199) for cooling and warming without formation of ice crystals were determined by plunging the solution into liquid nitrogen and then warming it in a water bath at 15 degrees C; when both glycerol and 1,2-propanediol were present in the solution (> 45% v/v), vitrification of the medium was observed. In Expt 2, IVM-IVF blastocysts were equilibrated to the mixture of glycerol and 1,2-propanediol (0% to 45%) at 15 degrees C in a stepwise manner as follows: (i) in one step, for 18 min to the final vitrification solution; (ii) in two steps, for 8 min in the first step and 10 min in the second step; (iii) in four steps, for 4 min in the first three steps and 6 min in the last step; (iv) in eight steps, for 2 min in each step, but 4 min in the last step; and (v) in 16 steps, for 1 min in each step, but 3 min in the last step. After removal of cryoprotectants, the blastocysts were cultured for 24 h in vitro. The survival rates for the embryos equilibrated in 1, 2, 4, 8 and 16 step(s) were 56, 89, 100, 100 and 100%, respectively. The blastocysts equilibrated in 1, 2, 4, 8 and 16 steps were vitrified by plunging the straws containing them into liquid N2, thawed and cultured in vitro.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2006

Repellency of oils of lemon eucalyptus, geranium, and lavender and the mosquito repellent MyggA natural to Ixodes ricinus (Acari: Ixodidae) in the laboratory and field.

MyggA Natural (Bioglan, Lund, Sweden) is a commercially available repellent against blood-feeding arthropods. It contains 30% of lemon-scented eucalyptus, Corymbia citriodora (Hook.) K. D. Hill & L. A. S. Johnson (Myrtaceae), oil with a minimum of 50% p-menthane-3,8-diol. MyggA Natural also contains small amounts of the essential oils of lavender, Lavandula angustifolia Mill. (Lamiaceae), and geranium, Pelargonium graveolens L'Her. (Geraniaceae). In laboratory bioassays, MyggA Natural and C. citriodora oil exhibited 100% repellency against host-seeking nymphs of Ixodes ricinus (L.) (Acari: Ixodidae). Lavender oil and geranium oil, when diluted to 1% in 1,2-propanediol, had weak repellent activities on I. ricinus nymphs, but when diluted to 30% in 1,2-propanediol had 100% repellencies. 1,2-Propanediol (100%) had no significant repellent activity in comparison with that of the control. In field tests in tick-infested areas in central Sweden, tick repellency of MyggA Natural and C. citriodora oil was tested by the blanket-dragging technique for 4 d during a 6-d period. The repellencies (74 and 85%, respectively) on day 1 are similar (89%) to that of blankets treated in a similar manner with 19% diethyl-methyl-benzamide, based on previous work. Repellencies declined significantly from day 1 to day 6 (74 to 45% for MyggA Natural; 85 to 42% for C. citriodora oil).

Animals↗
PubMed2005

Synthesis of acetals and ketals catalyzed by tungstosilicic acid supported on active carbon.

Catalytic activity of activated carbon supported tungstosilicic acid in synthesizing 2-methyl-2-ethoxycarbonylmethyl- 1,3-dioxolane, 2,4-dimethyl-2-ethoxycarbonylmethyl-1,3-dioxolane, cyclohexanone ethylene ketal, cyclohexanone 1,2-propa- nediol ketal, butanone ethylene ketal, butanone 1,2-propanediol ketal, 2-phenyl-1,3-dioxolane, 4-methyl-2-phenyl-1,3-dioxolane, 2-propyl-1,3-dioxolane, 4-methyl-2-propyl-1,3-dioxolane was reported. It has been demonstrated that activated carbon supported tungstosilicic acid is an excellent catalyst. Various factors involved in these reactions were investigated. The optimum conditions found were: molar ratio of aldehyde/ketone to glycol is 1/1.5, mass ratio of the catalyst used to the reactants is 1.0%, and reaction time is 1.0 h. Under these conditions, the yield of 2-methyl-2-ethoxycarbonylmethyl-1,3-dioxolane is 61.5%, of 2,4-dimethyl- 2-ethoxycarbonylmethyl-1,3-dioxolane is 69.1%, of cyclohexanone ethylene ketal is 74.6%, of cyclohexanone 1,2-propanediol ketal is 80.1%, of butanone ethylene ketal is 69.5%, of butanone 1,2-propanediol ketal is 78.5%, of 2-phenyl-1,3-dioxolane is 56.7%, of 4-methyl-2-phenyl-1,3-dioxolane is 86.2%, of 2-propyl-1,3-dioxolane is 87.5%, of 4-methyl-2-propyl-1,3-dioxolane is 87.9%.

Journal Article↗
PubMed1992

Identification and quantitative analysis of urinary metabolites of dichloropropanols in rats.

Urinary metabolites of dichloropropanols in rats were analyzed by gas chromatography-mass spectrometry (GC/MS). Solutions of dichloropropanols consisting of 1, 3-dichloro-2-propanol (DC2P) and 2, 3-dichloro-1-propanol (DC1P) were diluted in a saline at the concentration of 100 mg/ml, and 0.1 ml of the solutions were subcutaneously injected into male Wistar rats weighing about 160g. The urine samples were collected over a period of 24 hours after the injections. DC2P and DC1P in the urine were extracted with ethylacetate and analyzed by a GC/MS. The derivatization procedure with 4-bromophenylboric acid after acetonitril extraction was applied for the analyses of diols in the urine. By the GC/MS analysis, 3-chloro-1, 2-propanediol (3CPD), 2-chloro-1, 3-propanediol (2CPD) and 1, 2-propanediol (PPD) were identified as the hydroxylated metabolites of dichlorpropanols. Based on the analytical results, the metabolic pathways of dichlorpropanols forming 3CPD and 2CPD, and then hydroxylating to PPD were elucidated.

Animals↗
PubMed2000

A mechanistic approach to understanding species differences in felbamate bioactivation: relevance to drug-induced idiosyncratic reactions.

In an attempt to understand the species-selective toxicity of felbamate (2-phenyl-1,3-propanediol dicarbamate, FBM), which is thought to result from bioactivation to 2-phenylpropenal, FBM metabolism was evaluated in rats and humans. The formation of 2-phenylpropenal was monitored by the amount of its mercapturates excreted in urine. The data show a relative 5-fold increase in mercapturate excretion in patient urine as a result of differences in metabolism through P450-, esterase-, and aldehyde dehydrogenase-mediated pathways. To compensate for the significant species differences in FBM metabolism, and to produce toxic levels of 2-phenylpropenal in rat comparable to humans levels, monocarbamate felbamate (2-phenyl-1,3-propanediol monocarbamate, MCF), was administered to rats in the hopes of eliciting a toxic response. The desired result, an increase in mercapturate excretion, was not observed in MCF-treated rats due to the identification of a new FBM metabolite, 2-phenyl-1,3-propanediol monocarbamate-alpha-D-glucuronic acid (MCF-glucuronide). Formation of MCF-glucuronide is significant and represents about 80% of MCF metabolites in MCF-dosed rats, 3% of FBM metabolites in FBM-dosed rats, and about 11% of FBM metabolites in FBM patients. To overcome the protective effect of glucuronidation, uridine diphosphoglucuronosyltransferase (UGT)-deficient Gunn rats were treated with FBM and MCF, which surprisingly had no effect on the amount of MCF-glucuronide formed. Given the known UGT polymorphisms and the fact that MCF glucuronidation contributes to the elimination of a 2-phenylpropenal precursor, the correlation between poor UGT activity and an increase in mercapturates excretion was evaluated in patients. The result of the first 34 patients screened suggests that a patient with poor UGT activity is not necessarily at risk for FBM toxicity.

Animals↗
PubMed2003

[Study on the toxicological effect of chloropropanols on rats].

Toxicological effect of 3-chloro-1,2-propanediol on rats were studied to provide scientific basis for assessing the effect of Chloropropanols on human health. 170 SD rats were divided randomly into 8 groups and the dose of 0, 0.25, 0.5, 1.0, 2.0, 4.0, 8.0, 16.0 mg/kg 3-chloro-1,2-propanediol were given to rats for 90 days by gavages per day, respectively. The weight and food efficiency, hematology and clinical chemistry, NAG, GGT and total protein in urine, sperm number, sperm survive rate and sperm aberration rate, the LDH and LDH-X activity in testis, rate of organ/weight and histopathological analysis were measured. The results showed that different dose of 3-chloro-1,2-propanediol did not has adverse effect on body weight, food efficiency, Hb, red cell, white cell, serum AST, ALT, creatine, ALP, LDH, total protein and albumin, urine GGT and total protein, LDH activity in testis. At the dose of 4.0, 8.0 and 16.0 mg/kg group, the activity of NAG in urine and the rate of kidney/weight was significantly increased compared with negative control groups; the pathological changes in kidney were observed in the same groups, and the sperm number was also significantly decreased. At the dose of 8.0 and 16.0 mg/kg group, sperm survive rate and the X-LDH activity were significantly decreased and pathological changes were also observed in testis and caudal epididymis. It was concluded that the activity of NAG in urine and sperm number is the sensitive biological effective marker. Because urine is a kind of convenient available biological material, NAG activity in urine is a good biological effective marker for assessing effect of Chloropropanols on health. If the NAG activity can be used as sensitive marker for assessment on human health need to be tested further in human study.

Acetylglucosaminidase↗
PubMedDate not supplied

Felbamate metabolism in the rat, rabbit, and dog.

Two major and one minor metabolite of felbamate (FBM) as well as unchanged drug were isolated and identified by electron impact and chemical ionization mass spectrometry from rat and dog urine after dosing with [14C]FBM. The metabolites were 2-(4-hydroxyphenyl)-1,3-propanediol dicarbamate (p-OHF), 2-hydroxy-2-phenyl-1,3-propanediol dicarbamate, and 2-phenyl-1,3-propanediol monocarbamate. The metabolites and FBM were excreted mainly in urine, where their sum accounted to 81-94% of the radioactivity in hydrolyzed rat urine samples, 71-82% in rabbit urine samples, and 69-83% in dog urine samples. The amount of metabolites in the conjugated form was estimated to be 20-35% in rat, 20-30% in rabbit, and 10-20% in dog urine. The major biliary metabolite in all three species was p-OHF, whereas the amount of FBM was small. Metabolites found in dog feces were the same as those in the urine.

Animals↗
PubMed1991

1H NMR analyses of methyl group-containing metabolites in rat liver extracts--effects of starvation, anoxia, acute glycerol and carbon tetrachloride treatment and chronic ethanol administration on hepatic metabolism.

400 MHz 1H NMR spectroscopy was used to analyze methyl group-containing metabolites in perchloric acid extracts of livers of rats treated with carbon tetrachloride or fed with ethanol-containing liquid diets, and sacrificed with carbon dioxide anoxic euthanasia or pentobarbital euthanasia (with or without 12-18 hour fasting). In all cases, coenzyme A was detected using 1H NMR spectroscopy, but at higher levels for chronic ethanol-treated rats. Propionate was also detected in livers 6 hours after treatment with carbon tetrachloride. The assignments of the 1H NMR resonances in a spectrum of biological origin to these two metabolites have not been previously reported. Another unusual metabolite, 1,2-propanediol, was also observed in dramatically elevated levels in starved rats. The methyl groups for coenzyme A, propionate, and 1,2-propanediol have 1H NMR chemical shifts at 0.73 and 0.87 ppm, 1.18 ppm, and 1.14 ppm (from tetramethylsilane) respectively. In addition to the above mentioned resonances, glutamine, glutamate, proline, acetate, leucine, alanine, lactate, ethanol, beta-hydroxybutyrate, and valine were also observed in the 0.5-2.3 ppm methyl region of the 1H NMR spectra. Biochemical changes were also observed in these latter metabolites. beta-Hydroxybutyrate was increased by chronic ethanol administration; this increase was exacerbated by starvation. Alanine was decreased by chronic ethanol administration. Acetate was increased by chronic ethanol administration except when glycerol was added to the liver or when the rat was starved. We also observed an unassigned triplet at 0.81 ppm, and its appearance seems to be correlated with that of 1,2-propanediol.

Amino Acids↗
PubMed1986

Diol metabolism and diol dehydratase in Clostridium glycolicum.

Levels of the five enzymes involved in the fermentation of 1,2-ethanediol and 1,2-propanediol in the strictly anaerobic bacterium, Clostridium glycolicum, were investigated. All enzymes with the exception of the first enzyme in the pathway, diol dehydratase, were found to be constitutive, stable to exposure to oxygen, and present in the cytosol. Diol dehydratase was found to be extremely oxygen sensitive and strongly associated with the cell membrane. Treatment with ionic and nonionic detergents, butanol, phospholipase A2, or osmotic shock procedures failed to solubilize any diol dehydratase activity. Limited proteolysis using subtilisin released small amounts of activity. Diol dehydratase was found to be specific for 1,2-ethanediol and 1,2-propanediol and required the addition of a reducing agent for maximal activity. The enzyme was strongly inhibited by low concentrations of EDTA, ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid, o-phenanthroline, hydroxylamine, hydroxyurea, and sulfhydryl reagents. Addition of adenosylcobalamin or high levels of intrinsic factor did not affect the reaction rate. Irradiation with light also did not inhibit the enzyme activity. These results suggest that the catalytic mechanism of diol dehydratase from C. glycolicum does not involve a cobamide coenzyme.

Acetate Kinase↗
PubMed1979

Hydrogen transfer in catalysis by adenosylcobalamin-dependent diol dehydratase.

Studies [bachovchin, W. W., et al. (1978) Biochemistry 17, 2218] of the mechanism of inactivation of adenosylcobalamin-dependent diol dehydratase have led to the development of a general method to describe the kinetics of a reaction pathway containing a reservoir of mobile hydrogen. Analysis by this method of catalytic rate measurements for mixtures of 1,2-propanediol and 1,1-dideuterio-1,2-propanediol supports a mechanism involving an intermediate with three equivalent hydrogens, in which hydrogen transfer from this intermediate to product is the major rate-contributing step. Other results using tritium as a trace label [essenberg, M. K., et al. (1971) J. Am. Chem. Soc. 93, 1242] are considered in light of these deuterium isotope studies.

Cobamides↗
PubMed2002

Purification, characterization and subunits identification of the diol dehydratase of Lactobacillus collinoides.

The three genes pduCDE encoding the diol dehydratase of Lactobacillus collinoides, have been cloned for overexpression in the pQE30 vector. Although the three subunits of the protein were highly induced, no activity was detected in cell extracts. The enzyme was therefore purified to near homogeneity by ammonium sulfate precipitation and gel filtration chromatography. In fractions showing diol dehydratase activity, three main bands were present after SDS/PAGE with molecular masses of 63, 28 and 22 kDa, respectively. They were identified by mass spectrometry to correspond to the large, medium and small subunits of the dehydratase encoded by the pduC, pduD and pduE genes, respectively. The molecular mass of the native complex was estimated to 207 kDa in accordance with the calculated molecular masses deduced from the pduC, D, E genes (61, 24.7 and 19,1 kDa, respectively) and a alpha2beta2gamma2 composition. The Km for the three main substrates were 1.6 mm for 1,2-propanediol, 5.5 mm for 1,2-ethanediol and 8.3 mm for glycerol. The enzyme required the adenosylcobalamin coenzyme for catalytic activity and the Km for the cofactor was 8 micro m. Inactivation of the enzyme was observed by both glycerol and cyanocobalamin. The optimal reaction conditions of the enzyme were pH 8.75 and 37 degrees C. Activity was inhibited by sodium and calcium ions and to a lesser extent by magnesium. A fourth band at 59 kDa copurified with the diol dehydratase and was identified as the propionaldehyde dehydrogenase enzyme, another protein involved in the 1,2-propanediol metabolism pathway.

Chromatography, Gel↗
PubMed2003

Structural rationalization for the lack of stereospecificity in coenzyme B12-dependent diol dehydratase.

Adenosylcobalamin-dependent diol dehydratase of Klebsiella oxytoca is apparently not stereospecific and catalyzes the conversion of both (R)- and (S)-1,2-propanediol to propionaldehyde. To explain this unusual property of the enzyme, we analyzed the crystal structures of diol dehydratase in complexes with cyanocobalamin and (R)- or (S)-1,2-propanediol. (R)- and (S)-isomers are bound in a symmetrical manner, although the hydrogen-bonding interactions between the substrate and the active-site residues are the same. From the position of the adenosyl radical in the modeled "distal" conformation, it is reasonable for the radical to abstract the pro-R and pro-S hydrogens from (R)- and (S)-isomers, respectively. The hydroxyl groups in the substrate radicals would migrates from C(2) to C(1) by a suprafacial shift, resulting in the stereochemical inversion at C(1). This causes 60 degrees clockwise and 70 degrees counterclockwise rotations of the C(1)-C(2) bond of the (R)- and (S)-isomers, respectively, if viewed from K+. A modeling study of 1,1-gem-diol intermediates indicated that new radical center C(2) becomes close to the methyl group of 5'-deoxyadenosine. Thus, the hydrogen back-abstraction (recombination) from 5'-deoxyadenosine by the product radical is structurally feasible. It was also predictable that the substitution of the migrating hydroxyl group by a hydrogen atom from 5'-deoxyadenosine takes place with the inversion of the configuration at C(2) of the substrate. Stereospecific dehydration of the 1,1-gem-diol intermediates can also be rationalized by assuming that Asp-alpha335 and Glu-alpha170 function as base catalysts in the dehydration of the (R)- and (S)-isomers, respectively. The structure-based mechanism and stereochemical courses of the reaction are proposed.

Cloning, Molecular↗
PubMed1976

[An enzymic assay for the determination of vitamin B12 (author's transl)].

A procedure which extends the very sensitive propanediol-dehydratase reaction for 5'-deoxy-5'-adenosylcobalamine determination to cyanocobalamine and hydroxocobalamine is described. In this procedure, the cobalamines are adenosylated by vitamin B12 coenzyme synthetase and the resulting 5'-deoxy-5'-adenosylcobalamine can be determined by the propanediol-dehydratase reaction. Aldehyde, the product of the latter, can be registered by the alcohol dehydrogenase reaction.

Adenosine↗
PubMed1996

Secondary structure changes and peptic hydrolysis of beta-lactoglobulin induced by diols.

The addition of ethylene glycol, and 1,2- and 1,3-propanediol, decreases the bulk dielectric constant of the medium, and according to CD measurements, increases significantly the proportion of helical structure in beta-lactoglobulin. The medium-induced folding changes followed by limited peptic hydrolysis show that the cleavage of beta-lactoglobulin by pepsin is triggered by structural transformations induced by ethylene glycol only and not by 1, 2- and 1, 3-propanediol. Density measurements, at constant chemical potential and constant molality, demonstrate that all diols are present in the immediate domain of the protein. They are engaged in hydrophobic interactions with the amino acids of beta-lactoglobulin core inducing the formation of additional alpha-helices.

Alcohols↗