Synchrotron IR microspectroscopy for protein structure analysis: Potential and questions

Yu, Peiqiang

doi:10.1155/2006/263634

Title: Synchrotron IR microspectroscopy for protein structure analysis: Potential and questions

Full Record
Other Related Research

Abstract

Synchrotron radiation-based Fourier transform infrared microspectroscopy (S-FTIR) has been developed as a rapid, direct, non-destructive, bioanalytical technique. This technique takes advantage of synchrotron light brightness and small effective source size and is capable of exploring the molecular chemical make-up within microstructures of a biological tissue without destruction of inherent structures at ultra-spatial resolutions within cellular dimension. To date there has been very little application of this advanced technique to the study of pure protein inherent structure at a cellular level in biological tissues. In this review, a novel approach was introduced to show the potential of the newly developed, advanced synchrotron-based analytical technology, which can be used to localize relatively “pure“ protein in the plant tissues and relatively reveal protein inherent structure and protein molecular chemical make-up within intact tissue at cellular and subcellular levels. Several complex protein IR spectra data analytical techniques (Gaussian and Lorentzian multi-component peak modeling, univariate and multivariate analysis, principal component analysis (PCA), and hierarchical cluster analysis (CLA) are employed to relatively reveal features of protein inherent structure and distinguish protein inherent structure differences between varieties/species and treatments in plant tissues. By using a multi-peak modeling procedure, RELATIVE estimates (but not EXACT determinations) for protein secondarymore »« less

Authors:

Yu, Peiqiang ^[1]

College of Agriculture and Bioresources, University of Saskatchewan, 51 Campus Drive, Saskatoon, S7N 5A8, Canada, College of Agriculture and Bioresources, University of Saskatchewan, 6D34 Agriculture Building, 51 Campus Drive, Saskatoon, S7N 5A8, Canada

Publication Date:: Sun Jan 01 00:00:00 EST 2006

Sponsoring Org.:: USDOE

OSTI Identifier:: 1197994

Grant/Contract Number:: AC02-98CH10886

Resource Type:: Published Article

Journal Name:: Spectroscopy

Additional Journal Information:: Journal Name: Spectroscopy Journal Volume: 20 Journal Issue: 5,6; Journal ID: ISSN 0712-4813

Publisher:: Hindawi Publishing Corporation

Country of Publication:: Country unknown/Code not available

Language:: English

Citation Formats


                    Yu, Peiqiang. Synchrotron IR microspectroscopy for protein structure analysis: Potential and questions.  Country unknown/Code not available: N. p., 2006. 
Web.  doi:10.1155/2006/263634.

Copy to clipboard


                    Yu, Peiqiang. Synchrotron IR microspectroscopy for protein structure analysis: Potential and questions.  Country unknown/Code not available.  https://doi.org/10.1155/2006/263634

Copy to clipboard


                    Yu, Peiqiang. Sun .  
"Synchrotron IR microspectroscopy for protein structure analysis: Potential and questions".  Country unknown/Code not available.  https://doi.org/10.1155/2006/263634.

Copy to clipboard


                    
@article{osti_1197994,

  title        = {Synchrotron IR microspectroscopy for protein structure analysis: Potential and questions},

  author       = {Yu, Peiqiang},

  abstractNote = {Synchrotron radiation-based Fourier transform infrared microspectroscopy (S-FTIR) has been developed as a rapid, direct, non-destructive, bioanalytical technique. This technique takes advantage of synchrotron light brightness and small effective source size and is capable of exploring the molecular chemical make-up within microstructures of a biological tissue without destruction of inherent structures at ultra-spatial resolutions within cellular dimension. To date there has been very little application of this advanced technique to the study of pure protein inherent structure at a cellular level in biological tissues. In this review, a novel approach was introduced to show the potential of the newly developed, advanced synchrotron-based analytical technology, which can be used to localize relatively “pure“ protein in the plant tissues and relatively reveal protein inherent structure and protein molecular chemical make-up within intact tissue at cellular and subcellular levels. Several complex protein IR spectra data analytical techniques (Gaussian and Lorentzian multi-component peak modeling, univariate and multivariate analysis, principal component analysis (PCA), and hierarchical cluster analysis (CLA) are employed to relatively reveal features of protein inherent structure and distinguish protein inherent structure differences between varieties/species and treatments in plant tissues. By using a multi-peak modeling procedure, RELATIVE estimates (but not EXACT determinations) for protein secondary structure analysis can be made for comparison purpose. The issues of pro- and anti-multi-peaking modeling/fitting procedure for relative estimation of protein structure were discussed. By using the PCA and CLA analyses, the plant molecular structure can be qualitatively separate one group from another, statistically, even though the spectral assignments are not known. The synchrotron-based technology provides a new approach for protein structure research in biological tissues at ultraspatial resolutions.},

  doi          = {10.1155/2006/263634},

  journal      = {Spectroscopy},

  number       = 5,6,

  volume       = 20,

  place        = {Country unknown/Code not available},

  year         = {Sun Jan 01 00:00:00 EST 2006},

  month        = {Sun Jan 01 00:00:00 EST 2006}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1155/2006/263634

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 62 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Understanding the Differences in Molecular Conformation of Carbohydrate and Protein in Endosperm Tissues of Grains with Different Biodegradation Kinetics Using Advanced Synchrotron Technology

Journal Article Yu, P ; Block, H ; Doiron, K - Spectrochimica Acta, Part A

Conventional 'wet' chemical analyses rely heavily on the use of harsh chemicals and derivatization, thereby altering native seed structures leaving them unable to detect any original inherent structures within an intact tissue sample. A synchrotron is a giant particle accelerator that turns electrons into light (million times brighter than sunlight) which can be used to study the structure of materials at the molecular level. Synchrotron radiation-based Fourier transform IR microspectroscopy (SR-FTIRM) has been developed as a rapid, direct, non-destructive and bioanalytical technique. This technique, taking advantage of the brightness of synchrotron light and a small effective source size, is capablemore »« less
https://doi.org/10.1016/j.saa.2008.07.017
Plant-based Food and Feed Protein Structure Changes Induced by Gene-transformation heating and bio-ethanol processing: A Synchrotron-based Molecular Structure and Nutrition Research Program

Journal Article Yu, P - Molecular Nutrition and Food Research

Unlike traditional 'wet' analytical methods which during processing for analysis often result in destruction or alteration of the intrinsic protein structures, advanced synchrotron radiation-based Fourier transform infrared microspectroscopy has been developed as a rapid and nondestructive and bioanalytical technique. This cutting-edge synchrotron-based bioanalytical technology, taking advantages of synchrotron light brightness (million times brighter than sun), is capable of exploring the molecular chemistry or structure of a biological tissue without destruction inherent structures at ultra-spatial resolutions. In this article, a novel approach is introduced to show the potential of the advanced synchrotron-based analytical technology, which can be used to study plant-basedmore »« less
Characterization of the Microchemical Structure of Seed Endosperm within a Cellular Dimension among Six Barley Varieties with Distinct Degradation Kinetics, Using Ultraspatially Resolved Synchrotron-Based Infrared Synchrotron-Based Infrared

Journal Article Liu, N ; Yu, P - Journal of Agricultural and Food Chemistry

Barley varieties have similar chemical composition but exhibit different rumen degradation kinetics and nutrient availability. These biological differences may be related to molecular, structural, and chemical makeup among the seed endosperm tissue. No detailed study was carried out. The objectives of this study were: (1) to use a molecular spectroscopy technique, synchrotron-based Fourier transform infrared microspectroscopy (SFTIRM), to determine the microchemical-structural features in seed endosperm tissue of six developed barley varieties; (2) to study the relationship among molecular-structural characteristics, degradation kinetics, and nutrient availability in six genotypes of barley. The results showed that inherent microchemical-structural differences in the endosperm amongmore »« less
https://doi.org/10.1021/jf101233n
Molecular Basis of Protein Structure in Proanthocyanidin and Anthocyanin-Enhanced Lc-transgenic Alfalfa in Relation to Nutritive Value Using Synchrotron-Radiation FTIR Microspectroscopy: A Novel Approach

Journal Article Yu, P ; Jonker, A ; Gruber, M - Spectrochimica Acta, Part A

To date there has been very little application of synchrotron radiation-based Fourier transform infrared microspectroscopy (SRFTIRM) to the study of molecular structures in plant forage in relation to livestock digestive behavior and nutrient availability. Protein inherent structure, among other factors such as protein matrix, affects nutritive quality, fermentation and degradation behavior in both humans and animals. The relative percentage of protein secondary structure influences protein value. A high percentage of e-sheets usually reduce the access of gastrointestinal digestive enzymes to the protein. Reduced accessibility results in poor digestibility and as a result, low protein value. The objective of this studymore »« less
https://doi.org/10.1016/j.saa.2009.04.006
Ultra-Spatial Synchrotron Radiation for Imaging Molecular Chemical Structure: Applications in Plant and Animal Studies

Journal Article Yu, P - Spectroscopy

Synchrotron-based Fourier transform infrared microspectroscopy (S-FTIR) has been developed as a rapid, direct, non-destructive, bioanalytical technique. This technique takes advantage of synchrotron light brightness and small effective source size and is capable of exploring the molecular chemical features and make-up within microstructures of a biological tissue without destruction of inherent structures at ultra-spatial resolutions within cellular dimension. To date there has been very little application of this advanced synchrotron technique to the study of plant and animal tissues' inherent structure at a cellular or subcellular level. In this article, a novel approach was introduced to show the potential of themore »« less
https://doi.org/10.1155/2007/743101

Similar Records