Literature DB >> 7656562

The use and misuse of FTIR spectroscopy in the determination of protein structure.

M Jackson1, H H Mantsch.   

Abstract

Fourier transform infrared (FTIR) spectroscopy is an established tool for the structural characterization of proteins. However, many potential pitfalls exist for the unwary investigator. In this review we critically assess the application of FTIR spectroscopy to the determination of protein structure by (1) outlining the principles underlying protein secondary structure determination by FTIR spectroscopy, (2) highlighting the situations in which FTIR spectroscopy should be considered the technique of choice, (3) discussing the manner in which experiments should be conducted to derive as much physiologically relevant information as possible, and (4) outlining current methods for the determination of secondary structure from infrared spectra of proteins.

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Year:  1995        PMID： 7656562     DOI： 10.3109/10409239509085140

Source DB:  PubMed          Journal:  Crit Rev Biochem Mol Biol        ISSN： 1040-9238            Impact factor:   8.250


  235 in total

1.  Structures of yeast vesicle trafficking proteins.

Authors:  T Tishgarten; F F Yin; K M Faucher; R A Dluhy; T R Grant; G Fischer von Mollard; T H Stevens; L A Lipscomb
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

2.  Pressure versus temperature unfolding of ribonuclease A: an FTIR spectroscopic characterization of 10 variants at the carboxy-terminal site.

Authors:  J Torrent; P Rubens; M Ribó; K Heremans; M Vilanova
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

3.  Do parallel beta-helix proteins have a unique fourier transform infrared spectrum?

Authors:  R Khurana; A L Fink
Journal:  Biophys J       Date:  2000-02       Impact factor: 4.033

4.  Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution.

Authors:  R A Silva; J Kubelka; P Bour; S M Decatur; T A Keiderling
Journal:  Proc Natl Acad Sci U S A       Date:  2000-07-18       Impact factor: 11.205

5.  Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation.

Authors:  Melanie R Nilsson; Miles Driscoll; Daniel P Raleigh
Journal:  Protein Sci       Date:  2002-02       Impact factor: 6.725

6.  Single-domain antibody fragments with high conformational stability.

Authors:  Mireille Dumoulin; Katja Conrath; Annemie Van Meirhaeghe; Filip Meersman; Karel Heremans; Leon G J Frenken; Serge Muyldermans; Lode Wyns; Andre Matagne
Journal:  Protein Sci       Date:  2002-03       Impact factor: 6.725

7.  Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol.

Authors:  M J Paquet; M Laviolette; M Pézolet; M Auger
Journal:  Biophys J       Date:  2001-07       Impact factor: 4.033

8.  Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin.

Authors:  Filip Meersman; László Smeller; Karel Heremans
Journal:  Biophys J       Date:  2002-05       Impact factor: 4.033

9.  Primary folding dynamics of sperm whale apomyoglobin: core formation.

Authors:  Miriam Gulotta; Eduard Rogatsky; Robert H Callender; R Brian Dyer
Journal:  Biophys J       Date:  2003-03       Impact factor: 4.033

10.  Pressure- and temperature-induced unfolding and aggregation of recombinant human interferon-gamma: a Fourier transform infrared spectroscopy study.

Authors:  Koen Goossens; Joost Haelewyn; Filip Meersman; Marc De Ley; Karel Heremans
Journal:  Biochem J       Date:  2003-03-01       Impact factor: 3.857
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