Structural Information on Proteins from Circular Dichroism Spectroscopy Possibilities and Limitations

Bloemendal, Michael; Johnson, W. Curtis

doi:10.1007/978-1-4899-1079-0_2

Cited by 35 publications

(27 citation statements)

References 96 publications

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“…However, HPLC cannot quantify exclusively the amount of active antigen, as is the case with ELISA techniques 90. Changes in the secondary structure of a proteins are perhaps best monitored by CD spectroscopy 103. Finally, it is recommended to use several complementary analytical methods for the same protein formulation 36.…”

Section: Resultsmentioning

confidence: 99%

A Novel Approach to Prepare Insulin-Loaded Poly (Lactic-Co-Glycolic Acid) Microcapsules and the Protein Stability Study

Emami

Hamishehkar

Najafabadi

et al. 2009

Journal of Pharmaceutical Sciences

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Section: Resultsmentioning

confidence: 99%

A Novel Approach to Prepare Insulin-Loaded Poly (Lactic-Co-Glycolic Acid) Microcapsules and the Protein Stability Study

Emami

Hamishehkar

Najafabadi

et al. 2009

Journal of Pharmaceutical Sciences

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“…The program Varslc 1 was used to estimate the amount of secondary structures from CD data at 178-260 nm using a basis set of 33 proteins and singular value decomposition method of variable selection (Manavalan and Johnson, 1987 ;Bloemendal and Johnson, 1995).…”

Section: Methodsmentioning

confidence: 99%

Comparison of the Diphtheria Mutant Toxin, Crm197, with a Haemophilus Influenzae Type‐b Polysaccharide‐Crm197 Conjugate by Optical Spectroscopy

Crane

Bolgiano

Jones

1997

European Journal of Biochemistry

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A Haemophilus influenzae type-b capsular polysaccharide-CRM197 protein conjugate vaccine was compared with unconjugated CRM197 and diphtheria toxin, its parent molecule. Using CD and fluorescence spectroscopy, it has been possible to observe differences in structure and stability to pH and temperature due to the G52-E mutation in CRM197 and the 'glycosylation' of CRM197 in the conjugate. begins unfolding at slightly lower temperatures (25-35 "C) than native material (> 35 "C). In the conjugate, tryptophan residues are more accessible to the non-ionic flourescence quencher acrylamide at 35 "C. The conformational change observed at pH4-6 for diphtheria toxin is also observed for CRM197, but in the conjugate begins at higher pH. This may result from the presence of charged oligosaccharide residues on the surface or the conjugation methods used. The consequences of these changes in conformation and solution behaviour of the carrier protein in terms of its ability to induce a protective, T-celldependent response to H. influenzae polysaccharide remain to be determined.

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“…In the near UV region of the electromagnetic radiation spectrum (250-300 nm) only the aromatic residues of proteins (and to some extent disulfide bonds) absorb light, and this part of the spectrum reflects the tertiary structure of proteins [25]. A study of the effect of L-arginine on the secondary structure of the proteins was not possible due to Figure 11 shows the near UV CD spectra of pGH at 25°C in the buffer solution pH 7.5 without arginine and at two different arginine concentrations.…”

Section: Resultsmentioning

confidence: 99%

Probing of l-Arginine as an Additive for the Temperature-Induced Aggregation of Veterinary Growth Hormones: Fluorescence Study

Cirkovas

Sereikaitė

2011

Mol Biotechnol

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The influence of L-arginine on the temperature-induced aggregation of porcine and mink growth hormones was studied by fluorescence spectroscopy. It was found that L-arginine suppresses the heat-induced aggregation. Moreover, the analysis of L-arginine interaction with the native proteins by fluorescence spectroscopy and circular dichroism spectroscopy revealed no significant changes in their native structure. On the basis of the results, L-arginine could be considered as a potential additive for the prevention of storage and temperature-related denaturation and aggregation of veterinary growth hormones.

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Structural Information on Proteins from Circular Dichroism Spectroscopy Possibilities and Limitations

Cited by 35 publications

References 96 publications

A Novel Approach to Prepare Insulin-Loaded Poly (Lactic-Co-Glycolic Acid) Microcapsules and the Protein Stability Study

A Novel Approach to Prepare Insulin-Loaded Poly (Lactic-Co-Glycolic Acid) Microcapsules and the Protein Stability Study

Comparison of the Diphtheria Mutant Toxin, Crm197, with a Haemophilus Influenzae Type‐b Polysaccharide‐Crm197 Conjugate by Optical Spectroscopy

Probing of l-Arginine as an Additive for the Temperature-Induced Aggregation of Veterinary Growth Hormones: Fluorescence Study

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