2018
DOI: 10.1080/00387010.2018.1471092
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Investigation on the conformational changes of bovine serum albumin in a wide pH range from 2 to 12

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Cited by 30 publications
(18 citation statements)
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“…2 B, water has a strong IR absorbance around 1640 cm –1 (H–O–H bending), which overlaps with the Amide I mode of BSA (1700 cm –1 and 1600 cm –1 ). Despite these experimental challenges, we succeeded in acquiring BSA spectra over the pH range of interest here that could be used to characterize the BSA secondary structure because of the high signal/noise provided by the ATR-FTIR setup, as well previous studies 6 , 44 , 46 , 48 , 90 , 91 .…”
Section: Resultsmentioning
confidence: 99%
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“…2 B, water has a strong IR absorbance around 1640 cm –1 (H–O–H bending), which overlaps with the Amide I mode of BSA (1700 cm –1 and 1600 cm –1 ). Despite these experimental challenges, we succeeded in acquiring BSA spectra over the pH range of interest here that could be used to characterize the BSA secondary structure because of the high signal/noise provided by the ATR-FTIR setup, as well previous studies 6 , 44 , 46 , 48 , 90 , 91 .…”
Section: Resultsmentioning
confidence: 99%
“…Secondary structure can be determined by IR spectroscopy, because structural arrangements in the protein chain are associated with specific vibrational bands 38 46 . Besides IR, other techniques used to determine structure include X-ray crystallography 47 and UV-circular dichroism 46 , 48 50 .…”
Section: Introductionmentioning
confidence: 99%
“…The content of α helix was also calculated using molecular residue ellipticity (MRE) with OriginPro 2017 (OriginLab, Northampton, MA, USA). The content of α helix was estimated based on Equations (3) and (4) (similarly as in [11,39]),…”
Section: Methodsmentioning
confidence: 99%
“…There are several different approaches used for the evaluation of alpha helix content of a protein based on CD spectra changes. In Table 1, the results of two of them are summarized: Either the CD spectra evaluated by BeStSel algorithm (detailed structural changes shown in Table S1 (Supporting information)), or calculated values based on Equations (3) and (4) mentioned in the Experimental section (similarly as in [11,39]). Both approaches confirmed the reduction of α-helicity and simultaneous increase of other structures (like turn and random coil) in the course of AuNCs formation.…”
Section: Bsa Structural Changes In the Course Of Auncs Synthesismentioning
confidence: 99%
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