Structural Stability of Globulins

Shela Gorinstein; Marina Zemser; Octavio Paredes-López

doi:10.1021/jf9500849

Structural Stability of Globulins

Shela Gorinstein^*
, Marina Zemser
, Octavio Paredes-López

^*Corresponding author for this work

School of Pharmacy

Research output: Contribution to journal › Article › peer-review

52 Scopus citations

Abstract

Application of differential scanning calorimetry (DSC) and the susceptibility of amaranth globulins (A-G) to α-chymotrypsin gave a quantitative estimation of protein denaturation in solid state. To compare effects of size and crystal structure, A-G, quinoa globulins (Q-G), and bovine γ-globulins (γ-G) were examined at similar conditions for the extent of denaturation. A-G and Q-G showed similar data, but γ-G exhibited maximal conformational changes. The larger percentage of denaturation in globulins that is associated with enthalpy and the number of ruptured hydrogen bonds correspond to the smaller crystallinity determined by X-ray diffraction and disappearance of the α-helix in Fourier transform-infrared spectra.

Original language	English
Pages (from-to)	100-105
Number of pages	6
Journal	Journal of Agricultural and Food Chemistry
Volume	44
Issue number	1
DOIs	https://doi.org/10.1021/jf9500849
State	Published - Jan 1996

Keywords

Amaranth
Calorimetry
Denaturation
Quinoa
Spectroscopy

Access to Document

10.1021/jf9500849

Cite this

@article{7fac1e2e7ce64f81ada555eda959c157,

title = "Structural Stability of Globulins",

abstract = "Application of differential scanning calorimetry (DSC) and the susceptibility of amaranth globulins (A-G) to α-chymotrypsin gave a quantitative estimation of protein denaturation in solid state. To compare effects of size and crystal structure, A-G, quinoa globulins (Q-G), and bovine γ-globulins (γ-G) were examined at similar conditions for the extent of denaturation. A-G and Q-G showed similar data, but γ-G exhibited maximal conformational changes. The larger percentage of denaturation in globulins that is associated with enthalpy and the number of ruptured hydrogen bonds correspond to the smaller crystallinity determined by X-ray diffraction and disappearance of the α-helix in Fourier transform-infrared spectra.",

keywords = "Amaranth, Calorimetry, Denaturation, Quinoa, Spectroscopy",

author = "Shela Gorinstein and Marina Zemser and Octavio Paredes-L{\'o}pez",

year = "1996",

month = jan,

doi = "10.1021/jf9500849",

language = "אנגלית",

volume = "44",

pages = "100--105",

journal = "Journal of Agricultural and Food Chemistry",

issn = "0021-8561",

publisher = "American Chemical Society",

number = "1",

}

TY - JOUR

T1 - Structural Stability of Globulins

AU - Gorinstein, Shela

AU - Zemser, Marina

AU - Paredes-López, Octavio

PY - 1996/1

Y1 - 1996/1

N2 - Application of differential scanning calorimetry (DSC) and the susceptibility of amaranth globulins (A-G) to α-chymotrypsin gave a quantitative estimation of protein denaturation in solid state. To compare effects of size and crystal structure, A-G, quinoa globulins (Q-G), and bovine γ-globulins (γ-G) were examined at similar conditions for the extent of denaturation. A-G and Q-G showed similar data, but γ-G exhibited maximal conformational changes. The larger percentage of denaturation in globulins that is associated with enthalpy and the number of ruptured hydrogen bonds correspond to the smaller crystallinity determined by X-ray diffraction and disappearance of the α-helix in Fourier transform-infrared spectra.

AB - Application of differential scanning calorimetry (DSC) and the susceptibility of amaranth globulins (A-G) to α-chymotrypsin gave a quantitative estimation of protein denaturation in solid state. To compare effects of size and crystal structure, A-G, quinoa globulins (Q-G), and bovine γ-globulins (γ-G) were examined at similar conditions for the extent of denaturation. A-G and Q-G showed similar data, but γ-G exhibited maximal conformational changes. The larger percentage of denaturation in globulins that is associated with enthalpy and the number of ruptured hydrogen bonds correspond to the smaller crystallinity determined by X-ray diffraction and disappearance of the α-helix in Fourier transform-infrared spectra.

KW - Amaranth

KW - Calorimetry

KW - Denaturation

KW - Quinoa

KW - Spectroscopy

UR - https://www.scopus.com/pages/publications/0002980769

U2 - 10.1021/jf9500849

DO - 10.1021/jf9500849

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:0002980769

SN - 0021-8561

VL - 44

SP - 100

EP - 105

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 1

ER -

Structural Stability of Globulins

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this