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References from A convenient protein library for spectroscopic calibrations. Local targets link to admitted publications; unresolved targets remain external evidence.
Determination of the secondary structure of proteins in different environments by FTIR-ATR spectroscopy and PLS regression
10.1002/bip.21022 · 2008 · External reference
10.1021/bi00508a007
10.1021/bi00508a007 · External reference
Generation of a substructure library for the description and classification of protein secondary structure. II. Application to spectra-structure correlations in fourier transform infrared spectroscopy
10.1002/prot.340140405 · 1992 · External reference
Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra
1993 · External reference
The Optimization of Protein Secondary Structure Determination with Infrared and CD Spectra
2004 · External reference
Rationally selected basis proteins: A new approach to selecting proteins for spectroscopic secondary structure analysis
2003 · External reference
10.1093/bioinformatics/btr234
10.1093/bioinformatics/btr234 · External reference
10.1016/s0969-2126(97)00260-8
10.1016/s0969-2126(97)00260-8 · External reference
The Protein Data Bank: a computer-based archival file for macromolecular structures
10.1016/s0022-2836(77)80200-3 · 1977 · External reference
UniProt: the Universal Protein knowledgebase
10.1093/nar/gkh131 · 2004 · External reference
10.1016/0022-2836(70)90057-4
10.1016/0022-2836(70)90057-4 · External reference
10.1002/pro.3289
10.1002/pro.3289 · External reference
PDBsum: a web-based database of summaries and analyses of all PDB structures
10.1016/s0968-0004(97)01140-7 · 1997 · External reference
UniProt: a worldwide hub of protein knowledge
10.1093/nar/gky1049 · 2019 · External reference
Structural and Metal Binding Characterization of the C-Terminal Metallochaperone Domain of Membrane Fusion Protein SilB from Cupriavidus metallidurans CH34
10.1021/bi200005k · 2011 · External reference
Metal-induced Conformational Changes in ZneB Suggest an Active Role of Membrane Fusion Proteins in Efflux Resistance Systems
10.1073/pnas.1003908107 · 2010 · External reference
Structures of Intermediate Transport States of ZneA, a Zn(II)/proton Antiporter
2013 · External reference
10.1107/s0907444994014496
10.1107/s0907444994014496 · External reference
The Low Density Lipoprotein Receptor Active Conformation of Apolipoprotein E. Helix Organization in N-Terminal Domain-Phospholipid Disc Particles
10.1074/jbc.273.40.25825 · 1998 · External reference
10.1002/bip.360221211
10.1002/bip.360221211 · External reference
10.1016/s0969-2126(02)00700-1
10.1016/s0969-2126(02)00700-1 · External reference
10.1002/prot.10082
10.1002/prot.10082 · External reference
DSSPcont: continuous secondary structure assignments for proteins
10.1093/nar/gkg626 · 2003 · External reference
Quantitative IR spectrophotometry of peptides compounds in water (H2O) solutions. III. Estimation of the protein secondary structure
10.1002/bip.360301311 · 1990 · External reference
Estimation of the Number of Alpha-Helical and Beta-Strand Segments in Proteins Using Circular Dichroism Spectroscopy
10.1110/ps.8.2.370 · 1999 · External reference
10.1093/nar/gkl893
10.1093/nar/gkl893 · External reference
10.1016/j.jmb.2004.02.002
10.1016/j.jmb.2004.02.002 · External reference
Insights into protein structure and function from disorder-complexity space
10.1002/prot.21055 · 2006 · External reference
10.1007/s00018-010-0529-x
10.1007/s00018-010-0529-x · External reference
10.1042/bj20090379
10.1042/bj20090379 · External reference
10.1073/pnas.1500851112
10.1073/pnas.1500851112 · External reference
Infrared spectra and resonance interactions of amide-I and II vibrations of alpha-helix
10.1002/bip.1976.360150404 · 1976 · External reference
Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy
1994 · External reference
Infrared spectra and resonance interaction of amide-I vibration of the paraellel-chain pleated sheets
10.1002/bip.1976.360150403 · 1976 · External reference
Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
10.1002/bip.1975.360140402 · 1975 · External reference
Quantitative IR spectrophotometry of peptides compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption band
10.1002/bip.360301309 · 1991 · External reference
10.1016/s0079-6107(00)00021-3
10.1016/s0079-6107(00)00021-3 · External reference
10.1016/j.bbabio.2007.06.004
10.1016/j.bbabio.2007.06.004 · External reference
Secondary structure and membrane interaction of PR-39, a Pro+Arg-rich antibacterial peptide
1994 · External reference
Evaluation of the information content in infrared spectra for protein secondary structure determination
10.1529/biophysj.105.072017 · 2006 · External reference
Analysis of H-1/H-2 exchange kinetics using model infrared spectra
10.1366/000370204322729496 · 2004 · External reference
Analysis of biofluids in aqueous environment based on mid-infrared spectroscopy
10.1117/1.1917844 · 2005 · External reference
Unresolved reference
External reference
10.1021/acs.chemrev.9b00636
10.1021/acs.chemrev.9b00636 · External reference
Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
1999 · External reference
Secondary Structure Determination by Means of ATR-FTIR Spectroscopy
10.1007/978-1-4939-7151-0_10 · 2017 · External reference
Infrared imaging of high density protein arrays
10.1039/c6an02048h · 2017 · External reference
Analysis of protein microarrays by FTIR imaging
10.3233/bsi-160137 · 2016 · External reference
FTIR protein secondary structure analysis of human ascending aortic tissues
10.1002/jbio.200810020 · 2008 · External reference
Label-free classification of colon cancer grading using infrared spectral histopathology
10.1039/c5fd00157a · 2016 · External reference
A FTIR microspectroscopy study of the structural and biochemical perturbations induced by natively folded and aggregated transthyretin in HL-1 cardiomyocytes
10.1038/s41598-018-30995-5 · 2018 · External reference
10.1063/1.3429214
10.1063/1.3429214 · External reference
10.1002/0471721204.ch17
10.1002/0471721204.ch17 · External reference
10.1021/bi00699a002
10.1021/bi00699a002 · External reference
Dependence of alpha-helical and beta-sheet amino acid propensities on the overall protein fold type
10.1186/1472-6807-12-18 · 2012 · External reference
Protein secondary structure content in solution, films and tissues: Redundancy and complementarity of the information content in circular dichroism, transmission and ATR FTIR spectra
10.1016/j.bbapap.2009.06.007 · 2009 · External reference
10.1366/0003702963904610
10.1366/0003702963904610 · External reference
Hydrogen-deuterium exchange in membrane proteins monitored by IR spectroscopy: A new tool to resolve protein structure and dynamics
10.1002/bip.20035 · 2004 · External reference
Ruysschaert JM, de-Jongh HH. Amide-proton exchange of water-soluble proteins of different structural classes studied at the submolecular level by infrared spectroscopy
10.1021/bi971337p · 1997 · External reference
