Optical Activity of Proteins and Other Macromolecules

Jirgensons, B.

doi:10.1007/978-3-642-87713-1

Cited by 63 publications

(40 citation statements)

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“…. These interactions are accompanied by a transition to a more helical form of the protein, similar to that observed with proteins in the presence of the simpler amphiphile, sodium dodecyl sulfate [4,7,8].…”

Section: Introductionmentioning

confidence: 58%

“…This inability of the lipid to modify the polypeptide chain backbone conformation of the oLH subunits may be caused by two factors: 1) the rigidity of the macromolecule which is crosslinked by eleven disulfide bridges [ 10,13,14], and 2) by the high content of antihelix amino acids [ 13,141. The presence of carbohydrate [ 13,141 also is a factor deterring helix formation [4]. The effect of the synthetic phospholipid then was tested on solutions of native oLH.…”

Section: Resultsmentioning

confidence: 99%

“…The protein solution was mixed with the lipid dispersion, the mixtures left at room temperature (24-25°C) for 20-22 hr and the CD measurements made in a Durrum-JASCO improved CD-SP dichrograph as described previously [4,8]. The results are expressed as specific dichroism &iy~~, i.e.…”

Section: Methodsmentioning

confidence: 99%

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Effect of phospholipid on conformation of ovine luteinizing hormone as tested by circular dichroism

1974

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Section: Introductionmentioning

confidence: 58%

Section: Resultsmentioning

confidence: 99%

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Effect of phospholipid on conformation of ovine luteinizing hormone as tested by circular dichroism

1974

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“…Many applications to both organic and biological chemistry are compiled in SNATZKE's book [57]. Optical activity of proteins is discussed in JIRGENSONS [44], and CANTOR and TIMASHEFF [10], among others. Optical activity measurement of membrane fragments or vesicles is reviewed by WALLACH and WINZLER [75] and HOLZWARTH [40].…”

Section: B) Absorption Signals Using Polarized Lightmentioning

confidence: 99%

“…An optically active substance contains molecules or supramolecular structures which lack a certain aspect of symmetry; they cannot be superimposed to their own mirror images [5]. Nearly all biological molecules are optically active not only because of the existence of asymmetric carbon atoms but also because of foldings (such as helices) of primary chains ( [44], p. 17). Change in optical activity is therefore a very sensitive indicator of the change in conformation of the macromolecules ( [31], p. 573).…”

Section: B) Absorption Signals Using Polarized Lightmentioning

confidence: 99%

Mechanical, thermal, and optical changes of the nerve membrane associated with excitation.

Watanabe

1986

Jpn.J.Physiol

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In this minireview, some of the recent experimental findings on the excitable membranes of nerve fibers obtained by nonelectrophysiological means are discussed. This minireview, however, does not treat the vast literature on the "optical probes of the membrane potential," which is adequately covered by other excellent reviews [14,22,23,30,52].When the nerve fiber is excited, it transiently changes many of its physical properties. From the biological point of view, the most significant is the change in membrane potential, since the transmission of information along the nerve fiber is mediated by the electric local current. Other physical changes are significant mainly because they contain information on the molecular mechanism of the excitation process. They are usually very small for an easy detection, but progress in the techniques of extracting small signals from noise allowed us to discover and examine some of these signals. In this minireview, several recent findings on mechanical, thermal, and optical signals will be discussed.

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Protein conformation in bacterial spinae

Coombs¹,

Verpoorte²,

Easterbrook³

1976

Biopolymers

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SynopsisThe far uv circular dichroism (CD) and infrared spectra of bacterial spinae are reported. Estimates of the protein secondary structure were obtained by three-component curve-fitting methods supplemented by rank and factor analysis of CD data matrices. Native spinae were shown to contain approximately 88% antiparallel /%sheet, 7% a-helix, and 5% unordered structure based on estimates using poly(L-lysine). Basis CD spectra derived from globular proteins were shown to give unreliable estimates.

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Optical Activity of Proteins and Other Macromolecules

Cited by 63 publications

References 0 publications

Effect of phospholipid on conformation of ovine luteinizing hormone as tested by circular dichroism

Effect of phospholipid on conformation of ovine luteinizing hormone as tested by circular dichroism

Mechanical, thermal, and optical changes of the nerve membrane associated with excitation.

Protein conformation in bacterial spinae

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