Conformation and conformational stability of ribonuclease A and its peptic derivative, des-(121-124)-ribonuclease

Puett, David; Wasserman, Betty Kay; Friebele, Elaine

doi:10.1021/bi00760a038

Cited by 68 publications

(32 citation statements)

References 75 publications

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“…All samples were dissolved in 100 mM sodium phosphate buffer, pH 6.55. The reduced mean residue ellipticities ([ θ ] res ) were calculated taking in account that the mean residue molecular weight for pancreatic RNase A is 110.5 [17].…”

Section: Methodsmentioning

confidence: 99%

The two dimeric forms of RNase A

Sorrentino

Barone

Bucci³

et al. 2000

FEBS Letters

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In 1965 Fruchter and Crestfield (J. Biol. Chem. 240, 2868^3874) observed that dimeric RNase A prepared by lyophilization from acetic acid could be separated into two forms. Surprisingly, no other structural or functional differences could be detected between the two forms. In 1998 a structure for dimeric RNase A was determined by X-ray crystallography by Liu et al. (Proc. Natl. Acad. Sci. USA 95, 3437^3442). We found that the two forms of dimeric RNase A have indeed different structural and functional properties, and suggest that the dimer whose structure was investigated by Liu and coworkers may be identified with the lesser form of dimeric RNase A.z 2000 Federation of European Biochemical Societies.

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Section: Methodsmentioning

confidence: 99%

The two dimeric forms of RNase A

Sorrentino

Barone

Bucci³

et al. 2000

FEBS Letters

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“…Nevertheless, the positive maximum at 231 nm in AA has been assigned t o tyrosine residues (Kay, 1976). Similar assignments to tyrosine residues have been made for the 232nm band of human carbonic anhydrase B , the 234 nm bands of the 1.9 S soybean inhibitor and lima bean inhibitor , the 230nm band of ribonuclease A (Sinions & Blout, 1968;Pflum & Beychok, 1969;Puett, 1972). the 233nm band of the a-subunit of oLH (Bewley et a l , 1972a;Holladay & Puett, 1975), and the 228 nm band of cobrotoxin (Chen et al, 1977).…”

Section: Below 225nmmentioning

confidence: 64%

Circular Dichroism Spectra of Cleavage Fragments of Soybean Trypsin‐chymotrypsin Inhibitor

Birk¹,

Jibson²,

Bewley³

1980

International Journal of Peptide and Protein Research

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Circular dichroism spectra of biologically active fragments of Bowman‐Birk soybean inhibitor have been determined in acidic, neutral, and alkaline conditions. Neither fragment showed evidence of α‐helix or β‐structure. Negative dichroism above 260 nm has been assigned in both fragments primarily to disulfide bonds, with a minor contribution from tyrosine in a hydrophilic environment. The individual spectra of these fragments, and their sum between 230 and 340 nm have been compared with the spectra of the intact inhibitor and several structurally related proteins. Possible interactions which may give rise to CD bands in this region are discussed.

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“…The 232.5 positive CD extremum observed in ovine lutropin-a is reminiscent of a similar band in bovine pancreatic ribonuclease (Puett, 1972) and mouse submaxillary epidermal growth factor (Holladay et ul., 1976). Previously, we suggested that tyrosines 21 and 30 in ovine lutropin-a contribute significantly to this band.…”

Section: Peraturesmentioning

confidence: 88%

The EFFECTS OF DENATURANT AND TEMPERATURE ON THE CIRCULAR DICHROIC SPECTRUM OF OVINE LUTROPIN‐α

Puett

Holladay

1977

International Journal of Peptide and Protein Research

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Circular dichroic (CD) spectra of the glycoprotein hormone subunit, lutropin‐α, have been obtained under denaturing conditions (6 M guanidinium chloride, GdmCl) with the disulfides intact, reduced, and reduced and S‐carboxymethylated. Above 260 nm, these spectra are similar (although not identical), showing that the disulfide chromophores do not contribute appreciably to the near ultraviolet CD spectrum under denaturing conditions. However, these spectra differ considerably from that of native lutropin‐α over this spectral region demonstrating that the tertiary structure of lutropin‐α has a major influence on the near ultraviolet CD spectrum. The magnitude of the 232.5 nm positive CD extremum of lutropin‐α was found to increase with increasing GdmCl concentration and with decreasing temperature. Between 5d̀C and 45d̀C, the ellipticity [θ] at 232.5 nm changed in a linear fashion with temperature; at other wavelengths the thermal changes in [θ] were quite small. [θ] at 232.5 nm increased by about 80% over a 3 M GdmCl range; in contrast, [θ] at 216 nm (indicative of β‐structure) exhibited maximal changes over a 0.5 M GdmCl range. These results indicate some conformational flexibility in lutropin‐α. The positive 232.5 nm CD extremum has been assigned to one or more tyrosyls which are influenced by an intact disulfide. The latter was demonstrated by showing that reduced and S‐carboxymethylated lutropin‐α failed to exhibit the positive extremum.

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Conformation and conformational stability of ribonuclease A and its peptic derivative, des-(121-124)-ribonuclease

Cited by 68 publications

References 75 publications

The two dimeric forms of RNase A

The two dimeric forms of RNase A

Circular Dichroism Spectra of Cleavage Fragments of Soybean Trypsin‐chymotrypsin Inhibitor

The EFFECTS OF DENATURANT AND TEMPERATURE ON THE CIRCULAR DICHROIC SPECTRUM OF OVINE LUTROPIN‐α

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