New Fourier transform infrared based computational method for peptide secondary structure determination. I. Description of method

scientific article published in January 2001

New Fourier transform infrared based computational method for peptide secondary structure determination. I. Description of method is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/BIP.1002
P698PubMed publication ID11288058

P2093author name stringSimonetti M
Di Bello C
P2860cites workHigh-resolution three-dimensional structure of horse heart cytochrome cQ27668194
The Use and Misuse of FTIR Spectroscopy in the Determination of Protein StructureQ30417704
Evidence for beta-turn structure in model peptides reproducing pro-ocytocin/neurophysin proteolytic processing siteQ33821850
Amide modes and protein conformationQ35314453
Secondary structure of proteins through circular dichroism spectroscopyQ39653472
Vibrational spectroscopy and conformation of peptides, polypeptides, and proteinsQ39753611
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Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessmentQ40869927
Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. III. Estimation of the protein secondary structureQ41857691
Intensities and other spectral parameters of infrared amide bands of polypeptides in the ?- and random formsQ42080800
A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S.Q42661741
Determination of protein secondary structure using factor analysis of infrared spectraQ44595344
Conformational properties of azurin in solution as determined from resolution-enhanced Fourier-transform infrared spectra.Q50900998
Predictions of secondary structure using statistical analyses of electronic and vibrational circular dichroism and Fourier transform infrared spectra of proteins in H2O.Q52303132
Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods.Q52472482
CD and Fourier transform ir spectroscopic studies of peptides. II. Detection of beta-turns in linear peptides.Q53384999
Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in ?-, ?-, and random coil conformationsQ57223177
Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy waterQ66965932
Potential of carbon-13 and nitrogen-15 labeling for studying protein-protein interactions using Fourier-transform infrared spectroscopyQ67491871
Protein secondary structures in water from second-derivative amide I infrared spectraQ68458334
Intensities and other spectral parameters of infrared amide bands of polypeptides in the alpha-helical formQ68791748
Fourier transform infrared study of proteins with parallel beta-chainsQ69438789
Examination of the secondary structure of proteins by deconvolved FTIR spectraQ69484307
Resolution-enhanced Fourier transform infrared spectroscopy of enzymesQ69647499
Fourier transform infrared studies of ribonuclease in H2O and 2H2O solutionsQ69993945
Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bandsQ70265109
Characterization of beta-turns in cyclic hexapeptides in solution by Fourier transform IR spectroscopyQ70690205
Behavior of amphipathic helices on analysis via matrix methods, with application to glucagon, secretin, and vasoactive intestinal peptideQ71731905
Protein secondary structure from Fourier transform infrared and/or circular dichroism spectraQ72246110
CD conformational studies on synthetic peptides encompassing the processing domain of the ocytocin/neurophysin precursorQ73176602
Conformational studies on synthetic peptides reproducing the dibasic processing site of pro-ocytocin-neurophysinQ73510287
Predictions of protein secondary structures using factor analysis on Fourier transform infrared spectra: effect of Fourier self-deconvolution of the amide I and amide II bandsQ74476778
P433issue2
P304page(s)95-108
P577publication date2001-01-01
P1433published inBiopolymersQ15767528
P1476titleNew Fourier transform infrared based computational method for peptide secondary structure determination. I. Description of method
P478volume62

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cites work (P2860)
Q51457786Amide I vibrational circular dichroism of polypeptides: generalized fragmentation approximation method.
Q51959170Hydrogen-deuterium exchange in bovine serum albumin protein monitored by fourier transform infrared spectroscopy, part I: structural studies.
Q61871910On the specificity of the amide VI band for the secondary structure of proteins

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