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Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy

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Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy. / Ashton, Lorna; Dusting, Jonathan; Imomoh, Eboshogwe et al.

In: Biophysical Journal, Vol. 98, No. 4, 17.02.2010, p. 707-714.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Ashton, L, Dusting, J, Imomoh, E, Balabani, S & Blanch, EW 2010, 'Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy', Biophysical Journal, vol. 98, no. 4, pp. 707-714. https://doi.org/10.1016/bpj.2009.10.010

APA

Vancouver

Ashton L, Dusting J, Imomoh E, Balabani S, Blanch EW. Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy. Biophysical Journal. 2010 Feb 17;98(4):707-714. doi: 10.1016/bpj.2009.10.010

Author

Ashton, Lorna ; Dusting, Jonathan ; Imomoh, Eboshogwe et al. / Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy. In: Biophysical Journal. 2010 ; Vol. 98, No. 4. pp. 707-714.

Bibtex

@article{53663cf7a4724fcc865e41f2464c2fa9,
title = "Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy",
abstract = "By directly monitoring stirred protein solutions with Raman spectroscopy, the reversible unfolding of proteins caused by fluid shear is examined for several natural proteins with varying structural properties and molecular weight. While complete denaturation is not observed. a wide range of spectral variances occur for the different proteins, indicating subtle conformational changes that appear to be protein-specific A number of significant overall trends are apparent from the study For globular proteins, the overall extent of spectral variance increases with protein size and the proportion of beta-structure For two less structured proteins, fetuin and a-casein. the observed changes are of relatively low magnitude, despite the greater molecular structural mobility of these proteins This implies that other protein-specific factors, such as posttranslational modifications, may also be significant Individual band changes occurring in the spectral profiles of each individual protein are also discussed in detail",
keywords = "BETA-LACTOGLOBULIN, STRUCTURAL-CHARACTERIZATION, SECONDARY STRUCTURE, FILAMENTOUS VIRUS, CONCANAVALIN-A, SHEAR-FLOW, CASEIN, PHOSPHORYLATION, TRANSITION, FETUIN",
author = "Lorna Ashton and Jonathan Dusting and Eboshogwe Imomoh and Stavroula Balabani and Blanch, {Ewan W.}",
year = "2010",
month = feb,
day = "17",
doi = "10.1016/bpj.2009.10.010",
language = "English",
volume = "98",
pages = "707--714",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy

AU - Ashton, Lorna

AU - Dusting, Jonathan

AU - Imomoh, Eboshogwe

AU - Balabani, Stavroula

AU - Blanch, Ewan W.

PY - 2010/2/17

Y1 - 2010/2/17

N2 - By directly monitoring stirred protein solutions with Raman spectroscopy, the reversible unfolding of proteins caused by fluid shear is examined for several natural proteins with varying structural properties and molecular weight. While complete denaturation is not observed. a wide range of spectral variances occur for the different proteins, indicating subtle conformational changes that appear to be protein-specific A number of significant overall trends are apparent from the study For globular proteins, the overall extent of spectral variance increases with protein size and the proportion of beta-structure For two less structured proteins, fetuin and a-casein. the observed changes are of relatively low magnitude, despite the greater molecular structural mobility of these proteins This implies that other protein-specific factors, such as posttranslational modifications, may also be significant Individual band changes occurring in the spectral profiles of each individual protein are also discussed in detail

AB - By directly monitoring stirred protein solutions with Raman spectroscopy, the reversible unfolding of proteins caused by fluid shear is examined for several natural proteins with varying structural properties and molecular weight. While complete denaturation is not observed. a wide range of spectral variances occur for the different proteins, indicating subtle conformational changes that appear to be protein-specific A number of significant overall trends are apparent from the study For globular proteins, the overall extent of spectral variance increases with protein size and the proportion of beta-structure For two less structured proteins, fetuin and a-casein. the observed changes are of relatively low magnitude, despite the greater molecular structural mobility of these proteins This implies that other protein-specific factors, such as posttranslational modifications, may also be significant Individual band changes occurring in the spectral profiles of each individual protein are also discussed in detail

KW - BETA-LACTOGLOBULIN

KW - STRUCTURAL-CHARACTERIZATION

KW - SECONDARY STRUCTURE

KW - FILAMENTOUS VIRUS

KW - CONCANAVALIN-A

KW - SHEAR-FLOW

KW - CASEIN

KW - PHOSPHORYLATION

KW - TRANSITION

KW - FETUIN

U2 - 10.1016/bpj.2009.10.010

DO - 10.1016/bpj.2009.10.010

M3 - Journal article

VL - 98

SP - 707

EP - 714

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 4

ER -