Proposed rigidity of staphylococcal protease. Comments

Cm, Dobson

doi:10.1021/bi00693a019

Cited by 4 publications

(1 citation statement)

References 2 publications

(1 reference statement)

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“…It (25), and is also probably the origin of a similar resonance previously observed in proton NMR spectra of staphylococcal nuclease (26).…”

Section: Resultssupporting

confidence: 67%

Observation of individual carboxyl groups in hen egg-white lysozyme by use of high field 13C-nuclear magnetic resonance.

Shindo¹,

Cohen²

1976

Proc. Natl. Acad. Sci. U.S.A.

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13C-NMR studies of proteins is a complex function of several variables, and is discussed below.Carboxyl groups are vital both in terms of structure and function in proteins. The task of resolving their resonances is complicated by the presence of the many carbonyl resonances which absorb in the same region of the spectrum. However, we felt this to be a worthwhile study since there is no other means available to directly observe the properties of individual carboxyl groups in a protein in solution.Hen egg-white lysozyme (mucopeptide N-acetylmuramoyl hydrolase, EC 3.2.1.17) was chosen for this study not only because of its ready availability and stability, but also because it is known that the carboxyl groups of glutamic acid residue 35 and aspartic acid residue 52 are involved in its catalytic activity (7). One basis of our decision to attempt this study was the Noise-modulated proton decoupled, 13C-NMR spectra were obtained at 67.9 MHz with a superconducting magnet, on a Bruker WH-270 spectrometer equipped with a Fourier transform accessory, and a dedicated Raytheon 704 computer which gave 8000 real point transforms. A 900 radio frequency pulse (ca. 40 ,gsec) was applied and 30,000 transients were usually collected with a 2 sec recycle time. This accumulated transient signal was Fourier-transformed to give a spectrum with 15 kHz sweep width. Chemical shifts are reported in parts per million downfield from external tetramethylsilane, with D2O in a capillary as the NMR lock signal, at an ambient probe temperature of 40 I 2°.Curve-fitting was carried out with the Modeling Laboratory system on a PDP10 computer (Digital Equipment Corporation) at

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“…It (25), and is also probably the origin of a similar resonance previously observed in proton NMR spectra of staphylococcal nuclease (26).…”

Section: Resultssupporting

confidence: 67%

Observation of individual carboxyl groups in hen egg-white lysozyme by use of high field 13C-nuclear magnetic resonance.

Shindo¹,

Cohen²

1976

Proc. Natl. Acad. Sci. U.S.A.

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References

Govil¹,

Hosur²

1982

Conformation of Biological Molecules

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Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes

Talpas

Lee

1993

J Protein Chem

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The pKa values of His-38 and His-50 of the heparin-binding protein, bovine platelet factor 4, are 5.6 and 6.5, respectively, as determined by 1H NMR spectroscopy. The 1H NMR resonance of His-38 of bovine platelet factor 4 which exhibits the lower pKa value is perturbed upon heparin binding to a greater degree than the resonance of His-50. Human platelet factor 4 contains the homologous residues His-23 and His-35. The pKa values of the two histidine residues of human platelet factor 4 are 5.3 and 6.4. The 1H NMR resonance of the histidine of human platelet factor 4 exhibiting the lower pKa value also is perturbed upon heparin binding to a greater degree than the histidine resonance exhibiting the higher pKa, thereby suggesting comparable heparin-protein interactions in bovine and human platelet factor 4.

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Proposed rigidity of staphylococcal protease. Comments

Cited by 4 publications

References 2 publications

Observation of individual carboxyl groups in hen egg-white lysozyme by use of high field 13C-nuclear magnetic resonance.

Observation of individual carboxyl groups in hen egg-white lysozyme by use of high field 13C-nuclear magnetic resonance.

References

Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes

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