A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S

Haris, Parvez I.; Lee, Dong Hoon; Chapman, D.

doi:10.1016/0167-4838(86)90024-5

Cited by 144 publications

(128 citation statements)

References 38 publications

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“…More theoretical and experimental work is needed to clarify this point. However, the comparison of the frequencies of the component determined here and elsewhere for ribonucleases A and S [43] and for concanavalin A [44] points out a general similarity between the different analysis but also some differences. Splitting of the a-helix and the P-sheet component spontaneously occurs in the procedure described in this paper and can already yield important information for membrane proteins.…”

Section: Proteinsupporting

confidence: 57%

Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier‐transform infrared spectroscopy on hydrated films

Goormaghtigh

Cabiaux

Ruysschaert

1990

European Journal of Biochemistry

501

446

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Attenuated total reflection Fourier-transform infrared spectroscopy of thin hydrated films of soluble and membrane protein included in a phospholipid bilayer is shown to provide useful information as to the secondary structure of the protein. The analysis of the amide I band of deuterated samples by Fourier self-deconvolution followed by a curve fitting was performed by a new procedure in which all the input parameters are generated by the computer rather than by the investigator. The results of this analysis provide a correct estimation of the a-helix and P-sheet structure content with a standard deviation of 8.6% when X-ray structures are taken as a reference. We also show that the orientation of the different secondary structures resolved by the Fourier self-deconvolution/ curve-fitting procedure and of the phospholipid acyl chains can be simultaneously evaluated for membrane proteins reconstituted in a lipid bilayer. Of special interest for reconstitution of membrane proteins, the lipid/ protein ratio can be accurately and quickly determined from the infrared spectrum.Among the spectroscopic techniques currently used for the determination on secondary structures of proteins and peptides (circular dichroism, NMR, X-ray diffraction analysis, etc.) infrared spectroscopy has recently become a prominent one. Although its potential usefulness has been recognized for some time [l, 21, the recognition of the different components of conformation-sensitive amides bands (particularly amide I band) was difficult due to the resulting overlap of bands originating from the different secondary structures such as a-helix, P-sheet, p-turns and random. Pointing out the different components of amide I has been made possible by the advent of numerical analysis of the spectra. The computed second and fourth derivatives [3, 41 for instance replace a broad featureless band by peaks of well-resolved components. More recently, the use of Fourier self-deconvolution has provided the same type of result. The advantage of Fourier selfdeconvolution is that it does not change the integrated areas of the different components of the amide envelope [5]. It must be noted that the Fourier self-deconvolution does not achieve an actual resolution enhancement but rather enhances selected frequencies of the spectrum. The actual resolution of the spectrum is defined by the spectrophotometer settings. Once the number and the approximate frequency of the different components are known, curve-fitting procedures can be applied to quantify the area of the different components of the amide envelope (much care must be taken then to prevent the appearance of artefacts due to the numerical treatment). ItCorrespondence to E. Goormaghtigh, UniversitC Libre de Bruxelles, Campus Plaine CP 206/2, B-1050 Bruxelles, BelgiumAbbreviations. ATR, attenuated total reflection; FTIR, Fouriertransform infrared spectroscopy; Myr2GroPCho, dimyristoylphosphatidylcholine; OcGlc, octyl-glucopyranoside; FWHH, full width at half height.was only in 1986 that the first comprehensi...

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Section: Proteinsupporting

confidence: 57%

Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier‐transform infrared spectroscopy on hydrated films

Goormaghtigh

Cabiaux

Ruysschaert

1990

European Journal of Biochemistry

501

446

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“…1). The shift to lower wavenumbers of the amide I band maximum and the decrease in intensity of the amide II band at 1548 cm-' (observed in a *H,O medium) is due to the exchange of the amide hydrogens with deuterium [19,20]. Fig.…”

Section: Infrared Spectra Of Delipidated Andphospholipid Reconstitutementioning

confidence: 85%

Effect of neutral and acidic phospholipids on mitochondrial ATP synthase secondary structure

Sala¹,

Loregian²,

Lippe³

et al. 1993

FEBS Letters

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The secondary structure of delipidated and egg phosphatidylcholine or asolectin reconstituted mitochondrial ATP synthase complex from beef heart was investigated by Fourier transform infrared spectroscopy. Upon reconstitution, the infrared spectra of ATP synthase revealed an increase in turns and a concomitant decrease in p-sheet content which occurred to a larger extent in the presence of asolectin rather than in the presence of egg phosphatidylcholine. These data correlate with kinetic data showing a higher ATPase activity of the asolectin reconstituted enzyme protein than the egg phosphatidylcholine reconstituted or delipidated enzyme complexes.

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“…In this condition (without Mg 2+) the enzyme exchanged bound ATP with ADP and developed, during turnover, the hysteretic inhibition [6,7], characterised by an uninhibited initial rate which deceler- The shift value and the decrease in the amide II band intensity depend on the extent of H--~2H exchange [18,19] which, in turn, gives information on the accessibility of the solvent to the protein and on protein compactness. Fig.…”

Section: Conformation Of Fiatpase Obtained Using Buffer Containing Admentioning

confidence: 99%

Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F₁ATPase: a Fourier transform infrared spectroscopic study

et al. 1995

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Mitochondrial F~ATPase from beef heart was treated with different buffers in order to modulate the nucleotide content of the enzyme and then analysed by FT-IR spectroscopy. Treatment of F~ATPase with a buffer lacking nucleotides and glycerol led to the formation of two fractions consisting of an inactive aggregated enzyme deprived almost completely of bound nucleotides and of an active enzyme containing ATP only in the tight sites and having a structure largely accessible to the solvent and a low thermal stability. Treatment of F~ATPase with saturating ADP, which induced the hysteretic inhibition during turnover, or AMP-PNP did not affect remarkably the secondary structure of the enzyme complex but significantly increased its compactness and thermal stability. It was hypothesised that the formation of the inactive aggregated enzyme was mainly due to the destabilisation of the a-subunits of FtATPase and that the induction of the hysteretic inhibition is related to a particular conformation of the enzyme, which during turnover becomes unable to sustain catalysis.

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A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S

Cited by 144 publications

References 38 publications

Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier‐transform infrared spectroscopy on hydrated films

Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier‐transform infrared spectroscopy on hydrated films

Effect of neutral and acidic phospholipids on mitochondrial ATP synthase secondary structure

Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F₁ATPase: a Fourier transform infrared spectroscopic study

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A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S

Cited by 144 publications

References 38 publications

Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier‐transform infrared spectroscopy on hydrated films

Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier‐transform infrared spectroscopy on hydrated films

Effect of neutral and acidic phospholipids on mitochondrial ATP synthase secondary structure

Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F1ATPase: a Fourier transform infrared spectroscopic study

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Influence of ADP, AMP‐PNP and of depletion of nucleotides on the structural properties of F₁ATPase: a Fourier transform infrared spectroscopic study