Two-dimensional infrared spectroscopy: a promising new method for the time resolution of structures

Recently, new methods for determining time-evolving structures using infrared analogs of NMR spectroscopy have been introduced that have outstanding potential in structural biology. Already, within the past two years, structures of dipeptides, tripeptides and pentapeptides have been determined on mu...

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Bibliographic Details
Published inCurrent Opinion in Structural Biology Vol. 11; no. 5; pp. 516 - 522
Main Authors Zanni, Martin T, Hochstrasser, Robin M
Format Book Review Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.10.2001
Subjects
2D-IR
heterodyned
infrared
Models, Molecular
Molecular Structure
nonlinear
Nuclear Magnetic Resonance, Biomolecular
Oligopeptides - chemistry
peptide
photon echo
protein
Protein Conformation
Spectrophotometry, Infrared - methods
spectroscopy
Spectroscopy, Fourier Transform Infrared
structure
Two-dimensional
peptide
2D-IR
Two-dimensional
heterodyned
Plant biology
infrared
Biochemistry
nonlinear
structure
Techniques & Methods
spectroscopy
protein
photon echo
Structural biology
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Summary:Recently, new methods for determining time-evolving structures using infrared analogs of NMR spectroscopy have been introduced that have outstanding potential in structural biology. Already, within the past two years, structures of dipeptides, tripeptides and pentapeptides have been determined on much faster timescales than the conformational dynamics. Also, two-dimensional infrared correlation spectra of some proteins and isotopically edited alanine-rich helices have been examined.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ObjectType-Review-2
ISSN:0959-440X
1879-033X
DOI:10.1016/S0959-440X(00)00243-8