Structural characterization of a methionine-rich, emulsifying protein from sunflower seed

Maya J. Pandya; Richard B. Sessions; Phil B. Williams; Christopher E. Dempsey; Arthur S. Tatham; Peter R. Shewry; Anthony R. Clarke

doi:10.1002/(SICI)1097-0134(20000215)38:3<341::AID-PROT9>3.0.CO;2-D

Structural characterization of a methionine-rich, emulsifying protein from sunflower seed

Maya J. Pandya^*, Richard B. Sessions, Phil B. Williams, Christopher E. Dempsey, Arthur S. Tatham, Peter R. Shewry, Anthony R. Clarke

^*Corresponding author for this work

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

30 Citations (Scopus)

Abstract

The 2 S seed storage protein, sunflower albumin 8, contains an unusually high proportion of hydrophobic residues including 16 methionines in a mature protein of 103 amino acids. A structural model, based on the known structure of a related protein, has been constructed as a four-helix bundle cross- linked by four disulphide bonds. This model structure is consistent with data from circular dichroism and nuclear magnetic resonance experiments. Analysis of the model's surface shows the presence of a large hydrophobic face that may be responsible for the highly stable emulsions this protein is known to form with oil/water mixtures. (C) 2000 Wiley-Liss, Inc.

Original language	English
Pages (from-to)	341-349
Number of pages	9
Journal	Proteins: Structure, Function and Genetics
Volume	38
Issue number	3
DOIs	https://doi.org/10.1002/(SICI)1097-0134(20000215)38:3<341::AID-PROT9>3.0.CO;2-D
Publication status	Published - 15 Feb 2000
Externally published	Yes

Keywords

Emulsifying agent
Homology model
Hydrophobic face
Methionine-rich
Seed storage protein

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10.1002/(SICI)1097-0134(20000215)38:3<341::AID-PROT9>3.0.CO;2-D

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title = "Structural characterization of a methionine-rich, emulsifying protein from sunflower seed",

abstract = "The 2 S seed storage protein, sunflower albumin 8, contains an unusually high proportion of hydrophobic residues including 16 methionines in a mature protein of 103 amino acids. A structural model, based on the known structure of a related protein, has been constructed as a four-helix bundle cross- linked by four disulphide bonds. This model structure is consistent with data from circular dichroism and nuclear magnetic resonance experiments. Analysis of the model's surface shows the presence of a large hydrophobic face that may be responsible for the highly stable emulsions this protein is known to form with oil/water mixtures. (C) 2000 Wiley-Liss, Inc.",

keywords = "Emulsifying agent, Homology model, Hydrophobic face, Methionine-rich, Seed storage protein",

author = "Pandya, \{Maya J.\} and Sessions, \{Richard B.\} and Williams, \{Phil B.\} and Dempsey, \{Christopher E.\} and Tatham, \{Arthur S.\} and Shewry, \{Peter R.\} and Clarke, \{Anthony R.\}",

year = "2000",

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doi = "10.1002/(SICI)1097-0134(20000215)38:3<341::AID-PROT9>3.0.CO;2-D",

language = "English",

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journal = "Proteins: Structure, Function and Genetics",

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TY - JOUR

T1 - Structural characterization of a methionine-rich, emulsifying protein from sunflower seed

AU - Pandya, Maya J.

AU - Sessions, Richard B.

AU - Williams, Phil B.

AU - Dempsey, Christopher E.

AU - Tatham, Arthur S.

AU - Shewry, Peter R.

AU - Clarke, Anthony R.

PY - 2000/2/15

Y1 - 2000/2/15

N2 - The 2 S seed storage protein, sunflower albumin 8, contains an unusually high proportion of hydrophobic residues including 16 methionines in a mature protein of 103 amino acids. A structural model, based on the known structure of a related protein, has been constructed as a four-helix bundle cross- linked by four disulphide bonds. This model structure is consistent with data from circular dichroism and nuclear magnetic resonance experiments. Analysis of the model's surface shows the presence of a large hydrophobic face that may be responsible for the highly stable emulsions this protein is known to form with oil/water mixtures. (C) 2000 Wiley-Liss, Inc.

AB - The 2 S seed storage protein, sunflower albumin 8, contains an unusually high proportion of hydrophobic residues including 16 methionines in a mature protein of 103 amino acids. A structural model, based on the known structure of a related protein, has been constructed as a four-helix bundle cross- linked by four disulphide bonds. This model structure is consistent with data from circular dichroism and nuclear magnetic resonance experiments. Analysis of the model's surface shows the presence of a large hydrophobic face that may be responsible for the highly stable emulsions this protein is known to form with oil/water mixtures. (C) 2000 Wiley-Liss, Inc.

KW - Emulsifying agent

KW - Homology model

KW - Hydrophobic face

KW - Methionine-rich

KW - Seed storage protein

UR - https://www.scopus.com/pages/publications/0034651674

U2 - 10.1002/(SICI)1097-0134(20000215)38:3<341::AID-PROT9>3.0.CO;2-D

DO - 10.1002/(SICI)1097-0134(20000215)38:3<341::AID-PROT9>3.0.CO;2-D

M3 - Article

C2 - 10713993

AN - SCOPUS:0034651674

SN - 0887-3585

VL - 38

SP - 341

EP - 349

JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

IS - 3

ER -

Structural characterization of a methionine-rich, emulsifying protein from sunflower seed

Abstract

Keywords

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