RESUMO
Given the extensive use of fluorination in molecular design, it is imperative to understand the solvation properties of fluorinated compounds and the impact of the C-F bond on electrostatic interactions. Vibrational spectroscopy can provide direct insights into these interactions by using the C-F bond stretching [v(C-F)] as an electric field probe through the vibrational Stark effect (VSE). In this work, we explore the VSE of the three basic patterns of aliphatic fluorination, i.e., mono-, di-, and trifluorination in CF, CF2, and CF3 groups, respectively, and compare their response to the well-studied aromatic v(C-F). Magnitudes (i.e., Stark tuning rates) and orientations of the difference dipole vectors of the v(C-F)-containing normal modes were determined using density functional theory and a molecular dynamics (MD)-assisted solvatochromic analysis of model compounds in solvents of varying polarity. We obtain Stark tuning rates of 0.2-0.8 cm-1/(MV/cm), with smallest and largest electric field sensitivities for CFaliphatic and CF3,aliphatic, respectively. While average electric fields of solvation were oriented along the main symmetry axis of the CFn, and thus along its static dipole, the Stark tuning rate vectors were tilted by up to 87° potentially enabling to map electrostatics in multiple dimensions. We discuss the influence of conformational heterogeneity on spectral shifts and point out the importance of multipolar and/or polarizable MD force fields to describe the electrostatics of fluorinated molecules. The implications of this work are of direct relevance for studies of fluorinated molecules as found in pharmaceuticals, fluorinated peptides, and proteins.
RESUMO
Membrane proteins are molecular machines that transport ions, solutes, or information across the cell membrane. Electrophysiological techniques have unraveled many functional aspects of ion channels but suffer from the lack of structural sensitivity. Here, we present spectroelectrochemical data on vibrational changes of membrane proteins derived from a single monolayer. For the seven-helical transmembrane protein sensory rhodopsin II, structural changes of the protein backbone and the retinal cofactor as well as single ion transfer events are resolved by surface-enhanced IR difference absorption spectroscopy (SEIDAS). Angular changes of bonds versus the membrane normal have been determined because SEIDAS monitors only those vibrations whose dipole moment are oriented perpendicular to the solid surface. The application of negative membrane potentials (DeltaV = -0.3 V) leads to the selective halt of the light-induced proton transfer at the stage of D75, the counter ion of the retinal Schiff base. It is inferred that the voltage raises the energy barrier of this particular proton-transfer reaction, rendering the energy deposited in the retinal by light excitation insufficient for charge transfer to occur. The other structural rearrangements that accompany light-induced activity of the membrane protein, are essentially unaffected by the transmembrane electric field. Our results demonstrate that SEIDAS is a generic approach to study processes that depend on the membrane potential, like those in voltage-gated ion channels and transporters, to elucidate the mechanism of ion transfer with unprecedented spatial sensitivity and temporal resolution.
Assuntos
Ativação do Canal Iônico , Células Fotorreceptoras/química , Espectrofotometria Infravermelho/métodos , Luz , Potenciais da Membrana , Proteínas de Membrana/química , Conformação Proteica , Rodopsina/químicaRESUMO
A novel Fourier-transform infrared (FT-IR) rapid-scan spectrometer has been developed (patent pending EP14194520.4) which yields 1000 times higher time resolution as compared to conventional rapid-scanning spectrometers. The central element to achieve faster scanning rates is based on a sonotrode whose front face represents the movable mirror of the interferometer. A prototype spectrometer with a time resolution of 13 µs was realized, capable of fully automated long-term measurements with a flow cell for liquid samples, here a photosynthetic membrane protein in solution. The performance of this novel spectrometer is demonstrated by recording the photoreaction of bacteriorhodopsin initiated by a short laser pulse that is synchronized to the data recording. The resulting data are critically compared to those obtained by step-scan spectroscopy and demonstrate the relevance of performing experiments on proteins in solution. The spectrometer allows for future investigations of fast, non-repetitive processes, whose investigation is challenging to step-scan FT-IR spectroscopy.
RESUMO
Vibrational dynamics of the retinal all-trans to 13-cis photoisomerization in channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) was investigated by femtosecond visible pump mid-IR probe spectroscopy. After photoexcitation, the transient infrared absorption of C-C stretching modes was detected. The formation of the 13-cis photoproduct marker band at 1193 cm(-1) was observed within the time resolution of 0.3 ps. We estimated the photoisomerization yield to (60 ± 6) %. We found additional time constants of (0.55 ± 0.05) ps and (6 ± 1) ps, assigned to cooling, and cooling processes with a back-reaction pathway. An additional bleaching band demonstrates the ground-state heterogeneity of retinal.
RESUMO
Ultrashort flashes of THz light with low photon energies of a few meV, but strong electric or magnetic field transients have recently been employed to prepare various fascinating nonequilibrium states in matter. Here we present a new class of sources based on superradiant enhancement of radiation from relativistic electron bunches in a compact electron accelerator that we believe will revolutionize experiments in this field. Our prototype source generates high-field THz pulses at unprecedented quasi-continuous-wave repetition rates up to the MHz regime. We demonstrate parameters that exceed state-of-the-art laser-based sources by more than 2 orders of magnitude. The peak fields and the repetition rates are highly scalable and once fully operational this type of sources will routinely provide 1 MV/cm electric fields and 0.3 T magnetic fields at repetition rates of few 100 kHz. We benchmark the unique properties by performing a resonant coherent THz control experiment with few 10 fs resolution.
RESUMO
Bacteriorhodopsin is probably the best understood proton pump so far and is considered to be a model system for proton translocating membrane proteins. The basis of a molecular description of proton translocation is set by having the luxury of six highly resolved structural models at hand. Details of the mechanism and reaction dynamics were elucidated by a whole variety of biophysical techniques. The current molecular picture of catalysis by BR will be presented with examples from time-resolved spectroscopy. FT-IR spectroscopy monitors single proton transfer events within bacteriorhodopsin and judiciously positioned pH indicators detect proton migration at the membrane surface. Emerging properties are briefly outlined that underlie the efficient proton transfer across and along biological membranes.
Assuntos
Bacteriorodopsinas/química , Proteínas de Membrana/química , Bombas de Próton/química , Prótons , Membrana Purpúrea/química , Catálise , Cristalografia , Luz , Modelos Moleculares , Estrutura Terciária de Proteína , Espectroscopia de Infravermelho com Transformada de FourierRESUMO
Sensory rhodopsin II (SRII) from Halobacterium salinarum is heterologously expressed in Escherichia coli with a yield of 3-4 mg of purified SRII per liter cell culture. UV/Vis absorption spectroscopy display bands characteristic for native SRII. The resonance Raman spectrum provides evidence for a strongly hydrogen-bonded Schiff base like in mammalian rhodopsin but unlike to the homologous pSRII from Natronobacterium pharaonis. Laser flash spectroscopy indicates that SRII in detergent as well as after reconstitution into polar lipids shows its typical photochemical properties with prolonged photocycle kinetics. The first functional heterologous expression of SRII from H. salinarum provides the basis for studies with its cognate transducer HtrII to investigate the molecular processes involved in phototransduction as well as in chemotransduction.
Assuntos
Escherichia coli/genética , Halobacterium salinarum/genética , Rodopsinas Sensoriais/genética , Rodopsinas Sensoriais/metabolismo , Eletroforese , Cinética , Proteínas Recombinantes/genética , Proteínas Recombinantes/isolamento & purificação , Proteínas Recombinantes/metabolismo , Rodopsinas Sensoriais/isolamento & purificação , Análise Espectral RamanRESUMO
Unlike wild-type bacteriorhodopsin (BR), the BR triple mutant D96G/F171C/F219L has been shown to undergo only minor structural rearrangements during its photocycle. Nonetheless, the mutant is capable of transporting protons at a rate of 125(+/-40) H+/BR per minute under light-saturating conditions. Light adaptation of the triple mutant's retinal proceeds in a pH-dependent manner up to a maximum of 63% all-trans. These two findings imply that the transport activity of the triple mutant comprises 66% of the wild-type activity. Time-resolved spectroscopy reveals that the identity and sequence of intermediates in the photocycle of the triple mutant in the all-trans configuration correspond to that of wild-type BR. The only differences relate to a slower rise and decay of the M and O intermediates, and a significant spectral contribution from a 13-cis component. No indication for accumulation of the N intermediate is found under a variety of conditions that normally favor the formation of this species in wild-type BR. The Fourier transform infrared (FTIR) spectrum of the M intermediate in the triple mutant resembles that of wild type. Minor changes in the amide I region during the photocycle suggest that only small movements of the protein backbone occur. Electron microscopy reveals large differences in conformation between the unilluminated state of the mutant protein and wild-type but no light-induced changes in time-resolved measurements. Evidently, proton transport by the triple mutant does not require the major conformational rearrangements that occur on the same time-scale with wild-type. Thus, we conclude that large conformational changes observed in the photocycle of the wild-type and many BR mutants are not a prerequisite for the change in accessibility of the Schiff base nitrogen atom that must occur during vectorial catalysis to allow proton transport.
Assuntos
Archaea/química , Bacteriorodopsinas/química , Bacteriorodopsinas/metabolismo , Azidas/farmacologia , Bacteriorodopsinas/genética , Bacteriorodopsinas/ultraestrutura , Concentração de Íons de Hidrogênio , Transporte de Íons/efeitos dos fármacos , Transporte de Íons/efeitos da radiação , Isomerismo , Cinética , Luz , Microscopia Eletrônica , Mutação/genética , Fotólise/efeitos dos fármacos , Conformação Proteica/efeitos dos fármacos , Prótons , Retinaldeído/química , Retinaldeído/metabolismo , Espectroscopia de Infravermelho com Transformada de Fourier , Análise EspectralRESUMO
Hexagonal microcrystals of bacteriorhodopsin embedded in a lipidic cubic phase have been investigated by time-resolved FT-IR and resonance Raman spectroscopy. Retinal isomerization, conformational changes in the protein backbone and proton translocation are virtually indistinguishable from those in the native membrane. The protein is thus fully active in three-dimensional crystals.
Assuntos
Bacteriorodopsinas/química , Proteínas de Membrana/química , Amidas/química , Cristalização , Glicerídeos/metabolismo , Conformação Proteica , Prótons , Membrana Purpúrea/química , Retinaldeído/metabolismo , Espectroscopia de Infravermelho com Transformada de Fourier , Análise Espectral RamanRESUMO
The photocycle and the proton pumping kinetics of bacteriorhodopsin, as well as the transfer rate of protons from the membrane surface into the aqueous bulk phase were examined for purple membranes in water and ice. In water, the optical pH indicator pyranine residing in the aqueous bulk phase monitors the H(+)-release later than the pH indicator fluorescein covalently linked to the extracellular surface of BR. In the frozen state, however, pyranine responds to the ejected H+ as fast as fluorescein attached to BR, demonstrating that the surface/bulk transfer is in ice no longer rate limiting. The pumped H+ appears at the extracellular surface during the transition of the photocycle intermediate L550 to the intermediate M412. The Arrhenius plot of the M formation rate suggests that the proton is translocated through the protein via an ice-like structure.
Assuntos
Bacteriorodopsinas/química , Bacteriorodopsinas/fisiologia , Halobacterium/fisiologia , Transporte Biológico Ativo , Difusão , Concentração de Íons de Hidrogênio , Gelo , Cinética , LuzRESUMO
Attenuated total reflection (ATR) spectroscopy brings an added dimension to studies of structural changes of cytochrome c oxidase (CcO) because it enables the recording of reaction-induced infrared difference spectra under a wide variety of controlled conditions (e.g. pH and chemical composition), without relying on light or potentiometric changes to trigger the reaction. We have used the ATR method to record vibrational difference spectra of CcO with reduction induced by flow-exchange of the aqueous buffer. Films of CcO prepared from Rhodobacter sphaeroides and beef heart mitochondria by reconstitution with lipid were adhered to the internal reflection element of the ATR device and retained their full functionality as evidenced by visible spectroscopy and time-resolved vibrational spectroscopy. These results demonstrate that the technique of perfusion-induced Fourier-transform infrared difference spectroscopy can be successfully applied to a large, complex enzyme, such as CcO, with sufficient signal/noise to probe vibrational changes in individual residues of the enzyme under various conditions.
Assuntos
Complexo IV da Cadeia de Transporte de Elétrons/química , Complexo IV da Cadeia de Transporte de Elétrons/metabolismo , Espectroscopia de Infravermelho com Transformada de Fourier/métodos , Animais , Bovinos , Enzimas Imobilizadas/química , Enzimas Imobilizadas/metabolismo , Mitocôndrias Cardíacas/enzimologia , Oxirredução , Perfusão , Fosfolipídeos/química , Rhodobacter sphaeroides/enzimologia , VibraçãoRESUMO
The trapping function of the heterotopic splenic autotransplants (HSA) in 13 polytraumatized patients, aged 5-38 yr, was evaluated using heat damaged technetium-99m-labeled autologous red blood cells in early (1-7 mo) and late (3-4.5 yr) period after heterotopic autotransplantation to the omentum. The intensity of tracer accumulation was graded in comparison to the liver uptake. The splenic tissue surface was calculated on anterior projection each time. The shapes of the transplants were compared and new uptake foci suggesting spontaneous splenosis were looked for on both scans. The average surface of HSA was 28.2 (+/- 14.7) cm2 on early and 44.1 (+/- 14.3) cm2 on late examination (p less than 0.003) and the increase in intensity of tracer accumulation on both occasions was significant as well (p less than 0.0001). In three patients, some additional splenotic foci were found on follow-up scans. Howell-Jolly bodies in peripheral blood were detected in six of eight patients in early and remained detectable in lower number in three of eight patients on follow-up. No serious infection was noticed in our group of patients. Our work confirmed the excellent survival rates of HSA with improving trapping function and no important spread from original implantation site on long-term follow-up.
Assuntos
Reimplante , Baço/transplante , Ruptura Esplênica/cirurgia , Transplante Heterotópico , Adolescente , Adulto , Criança , Pré-Escolar , Feminino , Seguimentos , Humanos , Masculino , Omento , Ruptura Esplênica/epidemiologia , Fatores de TempoRESUMO
Rod photoreceptors contain three different glutamic acid-rich proteins (GARPs) that have been proposed to control the propagation of Ca(2+) from the site of its entry at the cyclic nucleotide-gated channel to the cytosol of the outer segment. We tested this hypothesis by measuring the binding of Ca(2+) to the following five constructs related to GARPs of rod photoreceptors: a 32-mer peptide containing 22 carboxylate groups, polyglutamic acid, a recombinant segment comprising 73 carboxylate groups (GLU), GARP1, and GARP2. Ca(2+) binding was investigated by means of a Ca(2+)-sensitive electrode. In all cases, Ca(2+) binds with low affinity; the half-maximum binding constant K(1/2) ranges from 6 to 16 mM. The binding stoichiometry between Ca(2+) ions and carboxylic groups is approximately 1:1; an exception is GARP2, where a binding stoichiometry of approximately 1:2 was found. Hydrodynamic radii of 1.6, 2.8, 3.3, 5.7, and 6.7 nm were determined by dynamic light scattering for the 32-mer, polyglutamic acid, GLU, GARP2, and GARP1 constructs, respectively. These results suggest that the peptides as well as GARP1 and GARP2 do not adopt compact globular structures. We conclude that the structures should be regarded as loose coils with low-affinity, high-capacity Ca(2+) binding.
Assuntos
Cálcio/química , Ácido Glutâmico/química , Proteínas do Tecido Nervoso/química , Peptídeos/química , Células Fotorreceptoras Retinianas Bastonetes/química , Sítios de Ligação , Ligação ProteicaRESUMO
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.
Assuntos
Bacteriorodopsinas/química , Bacteriorodopsinas/efeitos da radiação , Cristalografia/métodos , Espectroscopia de Infravermelho com Transformada de Fourier/métodos , Bacteriorodopsinas/ultraestrutura , Relação Dose-Resposta à Radiação , Cinética , Luz , Fotobiologia/métodos , Fotoquímica/métodos , Doses de Radiação , Fatores de TempoRESUMO
Proton transfer between water and the interior of membrane proteins plays a key role in bioenergetics. Here we survey the mechanism of this transfer as inferred from experiments with flash-triggered enzymes capturing or ejecting protons at the membrane surface. These experiments have revealed that proton exchange between the membrane surface and the bulk water phase proceeds at > or =1 msec because of a kinetic barrier for electrically charged species. From the data analysis, the barrier height for protons could be estimated as about 0.12 eV, i.e., high enough to account for the observed retardation in proton exchange. Due to this retardation, the proton activity at the membrane surface might deviate, under steady turnover of proton pumps, from that measured in the adjoining water phase, so that the driving force for ATP synthesis might be higher than inferred from the bulk-to-bulk measurements. This is particularly relevant for alkaliphilic bacteria. The proton diffusion along the membrane surface, on the other hand, is unconstrained and fast, occurring between the neighboring enzymes at less than 1 microsec. The anisotropy of proton dynamics at the membrane surface helps prokaryotes diminish the "futile" escape of pumped protons into the external volume. In some bacteria, the inner membrane is invaginated, so that the "ejected" protons get trapped in the closed space of such intracellular membrane "sacks" which can be round or flat. The chloroplast thylakoids and the mitochondrial cristae have their origin in these intracellular structures.
Assuntos
Metabolismo Energético/fisiologia , Membranas Intracelulares/química , Termodinâmica , Bactérias/química , Bactérias/metabolismo , Membranas Intracelulares/metabolismo , Transporte de Íons/fisiologia , Proteínas de Membrana/química , Proteínas de Membrana/metabolismo , Prótons , Propriedades de Superfície , Água/química , Água/metabolismoRESUMO
By comparing a mesophilic alpha-amylase with its thermophilic homolog, we investigated the relationship between thermal stability and internal equilibrium fluctuations. Fourier transform infrared spectroscopy monitoring hydrogen/deuterium (H/D) exchange kinetics and incoherent neutron scattering measuring picosecond dynamics were used to study dynamic features of the folded state at room temperature. Fairly similar rates of slowly exchanging amide protons indicate about the same free energy of stabilization DeltaG(stab) for both enzymes at room temperature. With respect to motions on shorter time scales, the thermophilic enzyme is characterized by an unexpected higher structural flexibility as compared to the mesophilic counterpart. In particular, the picosecond dynamics revealed a higher degree of conformational freedom for the thermophilic alpha-amylase. The mechanism proposed for increasing thermal stability in the present case is characterized by entropic stabilization and by flattening of the curvature of DeltaG(stab) as a function of temperature.
Assuntos
alfa-Amilases/química , alfa-Amilases/metabolismo , Bacillus/enzimologia , Cristalografia por Raios X , Cinética , Modelos Moleculares , Modelos Teóricos , Nêutrons , Estrutura Secundária de Proteína , Espalhamento de Radiação , Espectroscopia de Infravermelho com Transformada de Fourier , TermodinâmicaRESUMO
Light-induced H+ release and reuptake as well as surface potential changes inherent in the bacterio-rhodopsin reaction cycle were measured between 10 degrees C and 50 degrees C. Signals of optical pH indicators covalently bound to Lys-129 at the extracellular surface of bacteriorhodopsin were compared with absorbance changes of probes residing in the aqueous bulk phase. Only surface-bound indicators monitor the kinetics of H+ ejection from bacteriorhodopsin and allow the correlation of the photocycle with the pumping cycle. During the L550----M412 transition the H+ appears at the extracellular surface of bacteriorhodopsin. Surface potential changes detected by bound fluorescein or by the potentiometric probe 4-[2-(di-n-butylamino)-6-naphthyl]vinyl-1-(3-sulfopropyl)pyridinium betaine (di-4-ANEPPS) occur in milliseconds concomitantly with the formation and decay of the N intermediate. pH indicators residing in the aqueous bulk phase reflect the transfer of H+ from the membrane surface into the bulk but do not probe the early events of H+ pumping. The observed retardation of H+ at the membrane surface for several hundred microseconds is of relevance for energy conversion of biological membranes powered by electrochemical H+ gradients.
Assuntos
Bacteriorodopsinas/fisiologia , Potenciais da Membrana , Fotossíntese , Bacteriorodopsinas/química , Transporte Biológico , Membrana Celular/fisiologia , Fluoresceína , Fluoresceínas/química , Halobacterium salinarum , Concentração de Íons de Hidrogênio , Cinética , Luz , Espectrometria de FluorescênciaRESUMO
The photoreaction of the E194Q mutant of bacteriorhodopsin has been investigated at various pH values by time-resolved step-scan Fourier-transform infrared difference spectroscopy employing the attenuated total reflection technique. The difference spectrum at pH 8.4 is comparable to the N-BR difference spectra of the wild type with the remarkable exception that D85 is deprotonated. Since the retinal configuration is not perturbed by the E194Q mutation, it is concluded that there is no interaction of D85 with retinal during the lifetime of the N state. At pH 6, a consecutive state to the O intermediate is detected in which D212 is transiently protonated. The comparison with wild-type bacteriorhodopsin reveals that protonation of D212 represents an intermediate step during proton transfer from D85 to the proton release group in the final stage of the reaction cycle. The described effects are more pronounced in the E194Q mutant than in the E204Q mutant demonstrating different roles of these two glutamates/glutamic acids at least in the final stages of the catalytic cycle of bacteriorhodopsin.
Assuntos
Substituição de Aminoácidos , Bacteriorodopsinas/química , Bacteriorodopsinas/genética , Prótons , Espectroscopia de Infravermelho com Transformada de Fourier , Ácidos/química , Álcalis/química , Concentração de Íons de Hidrogênio , Mutação , Fotoquímica , Estrutura Secundária de Proteína , Estrutura Terciária de Proteína , Retinaldeído/química , Relação Estrutura-AtividadeRESUMO
The LOV1 domain of the blue light Phot1-receptor (phototropin homolog) from Chlamydomonas reinhardtii has been studied by vibrational spectroscopy. The FMN modes of the dark state of LOV1 were identified by preresonance Raman spectroscopy and assigned to molecular vibrations. By comparing the blue-light-induced FTIR difference spectrum with the preresonance Raman spectrum, most of the differences are due to FMN modes. Thus, we exclude large backbone changes of the protein that might occur during the phototransformation of the dark state LOV1-447 into the putative signaling state LOV1-390. Still, the presence of smaller amide difference bands cannot be excluded but may be masked by overlapping FMN modes. The band at 2567 cm(-1) is assigned to the S-H stretching vibration of C57, the residue that forms the transient thio-adduct with the chromophore FMN. The occurrence of this band is evidence that C57 is protonated in the dark state of LOV1. This result challenges conclusions from the homologous LOV2 domain from oat that the thiolate of the corresponding cysteine is the reactive species.
Assuntos
Chlamydomonas reinhardtii/química , Proteínas de Drosophila , Proteínas do Olho , Flavoproteínas/química , Flavoproteínas/efeitos da radiação , Células Fotorreceptoras de Invertebrados , Espectroscopia de Infravermelho com Transformada de Fourier/métodos , Análise Espectral Raman/métodos , Animais , Chlamydomonas reinhardtii/efeitos da radiação , Dicroísmo Circular/métodos , Cor , Criptocromos , Escuridão , Flavoproteínas/isolamento & purificação , Lasers , Luz , Conformação Molecular , Conformação Proteica , Estrutura Terciária de Proteína/efeitos da radiação , Receptores Acoplados a Proteínas G , Homologia de Sequência de AminoácidosRESUMO
Using a nonclinical and noneminent population, this study demonstrates an overlap in creative and schizotypal traits in the areas of perceptual functioning, behavioral and personality styles, and interests. No such overlap is observed in the area of divergent thinking. A battery containing five creativity measures was administered to a group of college student subjects scoring high on either the Perceptual Aberration Scale or the Magical Ideation Scale (N = 52) and to a group of control subjects (N = 65). A multivariate analysis of variance indicated that subjects high on the schizotypal traits of Perceptual Aberration or Magical Ideation (Per-Mag subjects) differed significantly from control subjects on the five creativity tests. Per-Mag subjects scored significantly higher than control subjects on the Barron-Welsh Revised Art Scale, a measure of preferences for figures, and the How Do You Think, a biographical and personality measure. There was a tendency for female Per-Mag subjects to score higher than female control subjects on the Domino Creativity Scale of the Adjective Check List. Per-Mag and control subjects did not differ on the Gough Creative Personality Scale of the Adjective Check List or on the Alternate Uses test, a test of divergent thinking. Per-Mag subjects who scored above the median for their group and gender on the Impulsive Nonconformity Scale received the highest creativity scores on the Barron-Welsh Revised Art Scale and the How Do You Think, although these results only approached significance. These findings argue for the specificity of areas of similarity and difference in schizotypy and creativity.