III. Montecastello

Kahn, François

doi:10.4000/books.aaccademia.2099

Cited by 4 publications

(7 citation statements)

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“…range (Fig. 1B) also results from contributions associated with tyrosine and the three disulphide bonds (26). The profiles confirm that the four proteins possess similar tertiary structures with the environments of tyrosine and cystine being conserved despite the different amino acid compositions (Table 1).…”

Section: Circular Dichroism Spectra Of Protease Inhibitorssupporting

confidence: 57%

“…The shoulder at 198 nm present in the spectrum of CSTI-IIb is likely to be associated with random coiled backbone; such profiles have been previously reported for proteins containing approximately 40% a-helix (20). The positive absorption in the 225-240nm region is associated with both the disulphide and tyrosine chromophores (26). Circular dichroism in the near U.V.…”

Section: Circular Dichroism Spectra Of Protease Inhibitorssupporting

confidence: 53%

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Structure analysis of trypsin inhibitors isolated from Cucurbitacae seeds. Circular dichroism studies

Hider¹,

Drake²,

Morrison³

et al. 1987

International Journal of Peptide and Protein Research

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Structure analysis jointly based on circular dichroism and Chou and Fasman analysis has been performed on a homologous group of 12 squash proteinase inhibitors. The analysis favours a structure incorporating 4 0 4 5 % helix which is tightly crosslinked by three disulphide bonds. The proposed structure is consistent with the previously published CD and 'H n.m.r. spectra. The amino acid which forms the centre of the interaction between trypsin and the inhibitor, arginine' or lysine', is located on the N-terminus of one of the helical segments. The basic residue is orientated away from the rest of the structure and thus is ideally situated for interaction with the confined space of the trypsin active site.

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Section: Circular Dichroism Spectra Of Protease Inhibitorssupporting

confidence: 57%

Section: Circular Dichroism Spectra Of Protease Inhibitorssupporting

confidence: 53%

Structure analysis of trypsin inhibitors isolated from Cucurbitacae seeds. Circular dichroism studies

Hider¹,

Drake²,

Morrison³

et al. 1987

International Journal of Peptide and Protein Research

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show abstract

“…In view of the large cystine or cysteine content of the external domain, there may be an underlying contribution from the disulphide bonds, its magnitude, sign and wavelength position depending on their geometry. The complexity of the near-UV spectrum renders interpretation in terms of individual components impossible (Kahn, 1979).…”

Section: Discussionmentioning

confidence: 99%

Epidermal growth factor binding induces a conformational change in the external domain of its receptor.

et al. 1989

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To study the properties of the extracellular epidermal growth factor (EGF) binding domain of the human EGF receptor, we have infected insect cells with a suitably engineered baculovirus vector containing the cDNA encoding the entire ectodomain of the parent molecule. This resulted in a correctly folded, stable, 110 kd protein which possessed an EGF binding affinity of 200 nM. The protein was routinely purified in milligram amounts from 1 litre insect cell cultures using a series of three standard chromatographic steps. The properties of the ectodomain were studied before and after the addition of different EGF ligands, using both circular dichroism and fluorescence spectroscopic techniques. A secondary structural analysis of the far UV CD spectrum of the ectodomain indicated significant proportions of alpha‐helix and beta‐sheet in agreement with a published model of the EGF receptor. The ligand additions to the receptor showed differences in both the near‐ and far‐UV CD spectra, and were similar for each ligand used, suggesting similar conformational differences between uncomplexed and complexed receptor. Steady‐state fluorescence measurements indicated that the tryptophan residues present in the ectodomain are buried and that the solvent‐accessible tryptophans in the ligands become buried on binding the receptor. The rotational correlation times measured by fluorescence anisotropy decay for the receptor‐ligand complexes were decreased from 6 to 2.5 ns in each case. This may indicate a perturbation of the tryptophan environment of the receptor on ligand binding. Ultracentrifugation studies showed that no aggregation occurred on ligand addition, so this could not explain the observed differences from CD or fluorescence.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…Both disulfide bridges ( 6 , 7 ) and B-turns (8,9) are important conformational determinants in biologically active peptides and proteins, stimulating interest in the spectro- scopic characterization of these structural features. The conformation of disulfide linkage is accessible to study, principally by circular dichroism (CD) (10) and Raman spectroscopy (1 1). Application of these techniques to peptides has been restricted by the relatively limited availability of suitable model systems.…”

mentioning

confidence: 99%

Cystine peptides.

Kishore

Ishizaki

et al. 1987

International Journal of Peptide and Protein Research

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NHCH3 (X = Gly 1, Ala 2, Aib 3, Leu 4 and D‐Ala 5), have been investigated by Raman and circular dichroism (CD) spectroscopy. Solid state Raman spectra are consistent with β‐turn conformations in all five peptides. These peptides exhibit similar conformations of the disulfide segment in the solid state with a characteristic disulfide stretching frequency at 519 ± 3 cm‐1, indicative of a trans‐gauche‐gauche arrangement about the Cα—Cβ—S—S—Cβ—Cα bonds. The results correlate well with the solid state conformations determined by X‐ray diffraction for peptides 3 and 4. CD studies in chloroform and dimethylsulfoxide establish solvent dependent conformational changes for peptides 1, 3 and 5. Disulfide chirality has been derived using the quadrant rule. CD results together with previously reported nuclear magnetic resonance (n.m.r.) data suggest a conformational coupling between the peptide backbone and the disulfide segment.

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III. Montecastello

Cited by 4 publications

References 0 publications

Structure analysis of trypsin inhibitors isolated from Cucurbitacae seeds. Circular dichroism studies

Structure analysis of trypsin inhibitors isolated from Cucurbitacae seeds. Circular dichroism studies

Epidermal growth factor binding induces a conformational change in the external domain of its receptor.

Cystine peptides.

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