Fourier transform infrared spectroscopic studies of the secondary structure and thermal denaturation of CaATPase from rabbit skeletal muscle

Jaworsky, Mark; Brauner, Joseph W.; Mendelsohn, Richard

doi:10.1016/0584-8539(86)80179-9

Cited by 14 publications

(6 citation statements)

References 29 publications

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“…For example, increases in the intensities of the bands at about 1600 cm À1 (i.e., the COO À antisymmetric stretches) were observed when Ca 2þ binds to bovine a-lactalbumin and equine lysosome [Mizuguchi et al, 1997]. Upon thermal denaturation, absorbance of the band at near 1630 cm À1 , assigned to ß-sheet structure, increases dramatically compared with the amide I feature in the area of 1655-1660 cm À1 , assigned to an a-helical and/ or random coil secondary structure [Jaworsky et al, 1986].…”

Section: Discussionmentioning

confidence: 97%

“…Several papers have reported the presence of a-helical secondary structure in the membrane transporter or other enzyme proteins [Brazier et al, 1998]. They show that intensities of amide I band are changed with an increase in temperature induced denaturation of enzymes such as (Ca 2þ þ Mg 2þ )-ATPase [Corbalán-García et al, 1994], CaATPase [Jaworsky et al, 1986] and Na, K ATPase [Heimburg et al, 1997]. Also, FT-IR spectroscopy has shown changes in a-helical structure to be a component of the difference between E 1 and E 2 states of Ca 2þ -ATPase and kinetics of folding/unfolding reaction of staphylococal nuclease by FT-IR spectroscopy [Panick et al, 1998].…”

Section: Discussionmentioning

confidence: 99%

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Effects of ELF magnetic field on membrane protein structure of living HeLa cells studied by Fourier transform infrared spectroscopy

Ikehara

Yamaguchi

Hosokawa

et al. 2003

Bioelectromagnetics

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The effects of exposure to a 50 Hz magnetic field (maximum of 41.7 to 43.6 mT) on the membrane protein structures of living HeLa cells were studied using attenuated total reflection infrared spectroscopy. One min of such exposure shifted peak absorbance of the amide I band to a smaller wave number, reduced peak absorbance of the amide II band, and increased absorbance at around 1600 cm(-1). These results suggest that exposure to the ELF magnetic field has reversible effects on the N-H inplane bending and C-N stretching vibrations of peptide linkages, and changes the secondary structures of alpha-helix and beta-sheet in cell membrane proteins.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Effects of ELF magnetic field on membrane protein structure of living HeLa cells studied by Fourier transform infrared spectroscopy

Ikehara

Yamaguchi

Hosokawa

et al. 2003

Bioelectromagnetics

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“…To optimize the resolution enhancement and to minimize spectral artifacts and distortion (Jaworsky et al, 1986) simultaneously, a bandwidth of 18 cm-' (full width at half height FWHH) and a resolution-enhancement factor (K value; Kauppinen et al, 1981a) of 2.6 were used.…”

Section: Selfdeconvolution and Spectral Analysismentioning

confidence: 99%

Fourier transform infrared spectroscopic study of Ca2+ and membrane-induced secondary structural changes in bovine prothrombin and prothrombin fragment 1

Wu¹,

Lentz²

1991

Biophysical Journal

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Fourier transform infrared (FTIR) spectroscopy was used to monitor secondary structural changes associated with binding of bovine prothrombin and prothrombin fragment 1 to acidic lipid membranes. Prothrombin and prothrombin fragment 1 were examined under four different conditions: in the presence of (a) Na2EDTA, (b) 5 mM CaCl2, and in the presence of CaCl2 plus membranes containing 1-palmitoyl-2-oleoyl-3-sn-phosphatidylcholine (POPC) in combination with either (c) bovine brain phosphatidyl-serine (bovPS) or (d) 1,2-dioleoyl-phosphatidylglycerol (DOPG). The widely reported Ca(2+)-induced conformational change in bovine prothrombin fragment 1 was properly detected by our procedures, although Ca(2+)-induced changes in whole prothrombin spectra were too small to be reliably interpreted. Binding of prothrombin in the presence of Ca2+ to procoagulant POPC/bovPS small unilamellar vesicles produced an increase in ordered secondary structures (2% and 3% increases in alpha-helix and beta-sheet, respectively) and a decrease of random structure (5%) as revealed by spectral analysis on both the original and Fourier-self-deconvolved data and by difference spectroscopy with the undeconvolved spectra. Binding to POPC/DOPG membranes, which are less active as procoagulant membranes, produced no detectable changes in secondary structure. In addition, no change in prothrombin fragment 1 secondary structure was detectable upon binding to either POPC/bovPS or POPC/DOPG membranes. This indicates that a membrane-induced conformational change occurs in prothrombin in the nonmembrane-binding portion of the molecule, part of which is activated to form thrombin, rather than in the membrane-binding fragment 1 region. The possible significance of this conformational change is discussed in terms of differences between the procoagulant activities of different acidic lipid membranes.

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“…The spectra have been subject to slight a phase whose DSC characteristics (Fig. 4) and FT-IR hancement (29), but no subtraction of the melting profiles ( Fig. 7) suggest it to be nearly pure ibsorption was attempted.…”

Section: Discussion Igh Temperature Transitions and A Resultantmentioning

confidence: 99%

“…In addition to information about lipid environments of CaATPase, the current results suggest a dependence on the lipid environment of the protein secondary structures achieved upon thermal denaturation. CaATPase in native SR (29) undergoes denaturation from a predominantly a-helical to a predominantly A-sheet form at 45°-50C, with no indication of additional major alterations in secondary structure as the temperature is raised. In contrast, the current study shows a second transition, from A-sheet to random coil, at temperatures that correspond to the melting of lipid domains enriched in DPPE-d62.…”

Section: Discussion Igh Temperature Transitions and A Resultantmentioning

confidence: 99%

Unusual partitioning behavior of CaATPase in dipalmitoylphosphatidylethanolamine/dielaidoylphosphatidylcholine++ + mixtures

Jaworsky

Mendelsohn

1987

Biophysical Journal

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CaATPase from rabbit sarcoplasmic reticulum has been isolated, purified, stripped of its native lipids, and reconstituted into binary lipid mixtures of dielaidoylphosphatidylcholine (DEPC) and dipalmitoylphosphatidylethanolamine (DPPE) or acyl-chain perdeuterated DPPE (DPPE-d62). The partitioning properties of the protein were determined from differential scanning calorimetry (DSC) and Fourier transform infrared (FT-IR) spectroscopy. Acyl-chain perdeuteration allows the separate determination of the order and melting characteristics of each lipid species with FT-IR. The binary lipid mixture has been shown to be phase separated in the gel state (Brauner, J. W., and R. Mendelsohn, 1986, Biochim. Biophys. Acta, 861:16-24). The solid phases present at low temperatures correspond to a pure DEPC phase and a mixed phase of DEPC/DPPE-d62. Insertion of protein at 37 degrees C leads to a domain of relatively protein-free DPPE-d62 and a phase containing both lipids plus CaATPase. We suggest that CaATPase selects a fixed composition (60% DEPC, 40% DPPE-d62) for its immediate environment. The composition of the lipid in the immediate vicinity of protein is largely independent of the initial DEPC/DPPE-d62 ratios in the reconstitution protocol. The relevance of these results to observations of discrete domains in native membranes is discussed.

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Fourier transform infrared spectroscopic studies of the secondary structure and thermal denaturation of CaATPase from rabbit skeletal muscle

Cited by 14 publications

References 29 publications

Effects of ELF magnetic field on membrane protein structure of living HeLa cells studied by Fourier transform infrared spectroscopy

Effects of ELF magnetic field on membrane protein structure of living HeLa cells studied by Fourier transform infrared spectroscopy

Fourier transform infrared spectroscopic study of Ca2+ and membrane-induced secondary structural changes in bovine prothrombin and prothrombin fragment 1

Unusual partitioning behavior of CaATPase in dipalmitoylphosphatidylethanolamine/dielaidoylphosphatidylcholine++ + mixtures

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