Literature DB >> 2085660

Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands.

N N Kalnin.   

Abstract

Infrared spectra of the amino acid residues in H2O solution have been obtained in the 1800-1400-cm-1 region. It has been established that amino acid residues of arginine, asparagine, glutamine, aspartic and glutamic acids, lysine, tyrosine, histidine, and phenylalanine have intensive absorption in this spectral region. Infrared spectra for a set of model compounds have been measured. On the basis of these data, spectral parameters of amino acid residue absorption bands have been determined.

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Year:  1990        PMID: 2085660     DOI: 10.1002/bip.360301309

Source DB:  PubMed          Journal:  Biopolymers        ISSN: 0006-3525            Impact factor:   2.505


  90 in total

1.  Structural changes of the sarcoplasmic reticulum Ca(2+)-ATPase upon nucleotide binding studied by fourier transform infrared spectroscopy.

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

Authors:  R Khurana; A L Fink
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3.  Quantitation of secondary structure in ATR infrared spectroscopy.

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Journal:  Biophys J       Date:  1999-11       Impact factor: 4.033

4.  C-deuterated alanine: a new label to study membrane protein structure using site-specific infrared dichroism.

Authors:  Jaume Torres; Isaiah T Arkin
Journal:  Biophys J       Date:  2002-02       Impact factor: 4.033

5.  Characterization of a new caged proton capable of inducing large pH jumps.

Authors:  Andreas Barth; John E T Corrie
Journal:  Biophys J       Date:  2002-11       Impact factor: 4.033

6.  Structural and functional implications of the instability of the ADP/ATP transporter purified from mitochondria as revealed by FTIR spectroscopy.

Authors:  Víctor A Lórenz-Fonfría; Joaquim Villaverde; Véronique Trézéguet; Guy J-M Lauquin; Gérard Brandolin; Esteve Padrós
Journal:  Biophys J       Date:  2003-07       Impact factor: 4.033

7.  Rationally selected basis proteins: a new approach to selecting proteins for spectroscopic secondary structure analysis.

Authors:  Keith A Oberg; Jean-Marie Ruysschaert; Erik Goormaghtigh
Journal:  Protein Sci       Date:  2003-09       Impact factor: 6.725

Review 8.  FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model.

Authors:  K J Rothschild
Journal:  J Bioenerg Biomembr       Date:  1992-04       Impact factor: 2.945

9.  Structural comparison of metarhodopsin II, metarhodopsin III, and opsin based on kinetic analysis of Fourier transform infrared difference spectra.

Authors:  A L Klinger; M S Braiman
Journal:  Biophys J       Date:  1992-11       Impact factor: 4.033

10.  In situ ATR-IR spectroscopic and electron microscopic analyses of settlement secretions of Undaria pinnatifida kelp spores.

Authors:  L Petrone; R Easingwood; M F Barker; A J McQuillan
Journal:  J R Soc Interface       Date:  2010-08-04       Impact factor: 4.118

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