Force-Induced Structural Changes in Spider Silk Fibers Introduced by ATR-FTIR Spectroscopy

[1]  N. Pugno,et al.  Impact of physio-chemical spinning conditions on the mechanical properties of biomimetic spider silk fibers , 2022, Communications Materials.

[2]  D. Kaplan,et al.  1000 spider silkomes: Linking sequences to silk physical properties , 2022, Science advances.

[3]  H. Schniepp,et al.  Protein secondary structure in spider silk nanofibrils , 2022, Nature Communications.

[4]  N. Pugno,et al.  Engineered Spider Silk Proteins for Biomimetic Spinning of Fibers with Toughness Equal to Dragline Silks , 2022, Advanced functional materials.

[5]  N. Pugno,et al.  Artificial and natural silk materials have high mechanical property variability regardless of sample size , 2022, Scientific Reports.

[6]  N. Pugno,et al.  High-yield production of a super-soluble miniature spidroin for biomimetic high-performance materials , 2021, Materials Today.

[7]  T. Asakura.  Structure of Silk I (Bombyx mori Silk Fibroin before Spinning) -Type II β-Turn, Not α-Helix- , 2021, Molecules.

[8]  J. Johansson,et al.  Tyrosine residues mediate supercontraction in biomimetic spider silk , 2021, Communications Materials.

[9]  E. Goormaghtigh,et al.  Amino acid side chain contribution to protein FTIR spectra: impact on secondary structure evaluation , 2021, European Biophysics Journal.

[10]  Kenjiro Yazawa,et al.  Pressure- and humidity-induced structural transition of silk fibroin , 2020, Polymer.

[11]  M. Steel,et al.  Transformation of aqueous protein attenuated total reflectance infra-red absorbance spectroscopy to transmission , 2020, QRB Discovery.

[12]  J. Popp,et al.  The Bouguer‐Beer‐Lambert Law: Shining Light on the Obscure , 2020, Chemphyschem : a European journal of chemical physics and physical chemistry.

[13]  A. Barth,et al.  On the Secondary Structure of Silk Fibroin Nanoparticles Obtained Using Ionic Liquids: An Infrared Spectroscopy Study , 2020, Polymers.

[14]  Maosen Xu,et al.  Mechanical properties and application analysis of spider silk bionic material , 2020 .

[15]  I. Leito,et al.  Reflectance FT-IR spectroscopy as a viable option for textile fiber identification , 2019, Heritage Science.

[16]  P. Baglioni,et al.  Understanding the structural degradation of South American historical silk: A Focal Plane Array (FPA) FTIR and multivariate analysis , 2019, Scientific Reports.

[17]  P. Wormell,et al.  Infrared absorbance spectroscopy of aqueous proteins: Comparison of transmission and ATR data collection and analysis for secondary structure fitting , 2018, Chirality.

[18]  Zhipeng He,et al.  Low pressure‐induced secondary structure transitions of regenerated silk fibroin in its wet film studied by time‐resolved infrared spectroscopy , 2018, Proteins.

[19]  G. Plaza,et al.  Biomimetic spinning of artificial spider silk from a chimeric minispidroin. , 2017, Nature chemical biology.

[20]  I. Leito,et al.  Identification and classification of textile fibres using ATR-FT-IR spectroscopy with chemometric methods. , 2017, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

[21]  Jinrong Yao,et al.  Insights into Silk Formation Process: Correlation of Mechanical Properties and Structural Evolution during Artificial Spinning of Silk Fibers. , 2016, ACS biomaterials science & engineering.

[22]  Ewan W Blanch,et al.  Determination of Protein Secondary Structure from Infrared Spectra Using Partial Least-Squares Regression. , 2016, Biochemistry.

[23]  C. Holland,et al.  Identification and classification of silks using infrared spectroscopy , 2015, Journal of Experimental Biology.

[24]  Yuan Cheng,et al.  Structures, mechanical properties and applications of silk fibroin materials , 2015 .

[25]  F. Severcan,et al.  Phylogeny of cultivated and wild wheat species using ATR-FTIR spectroscopy. , 2015, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

[26]  I. Ilev,et al.  Grazing incidence angle based sensing approach integrated with fiber-optic Fourier transform infrared (FO-FTIR) spectroscopy for remote and label-free detection of medical device contaminations. , 2014, The Review of scientific instruments.

[27]  Rohit Bhargava,et al.  Using Fourier transform IR spectroscopy to analyze biological materials , 2014, Nature Protocols.

[28]  A. Percot,et al.  Water dependent structural changes of silk from Bombyx mori gland to fibre as evidenced by Raman and IR spectroscopies , 2014 .

[29]  F. Kremer,et al.  Pressure-Dependent FTIR-Spectroscopy on the Counterbalance between External and Internal Constraints in Spider Silk of Nephila pilipes , 2013 .

[30]  M. Burghammer,et al.  Structure changes in Nephila dragline: The influence of pressure , 2012 .

[31]  F. Kremer,et al.  Supercontraction in Nephila spider dragline silk - Relaxation into equilibrium state , 2011 .

[32]  B. Desbat,et al.  Orientation of molecular groups of fibers in nonoriented samples determined by polarized ATR-FTIR spectroscopy , 2011, Analytical and bioanalytical chemistry.

[33]  Z. Shao,et al.  Synchrotron FTIR microspectroscopy of single natural silk fibers. , 2011, Biomacromolecules.

[34]  Rohit Bhargava,et al.  Theory of infrared microspectroscopy for intact fibers. , 2011, Analytical chemistry.

[35]  Thierry Buffeteau,et al.  Quantitative determination of band distortions in diamond attenuated total reflectance infrared spectra. , 2010, The journal of physical chemistry. B.

[36]  T. Lefèvre,et al.  Attenuated Total Reflection Infrared Spectroscopy: An Efficient Technique to Quantitatively Determine the Orientation and Conformation of Proteins in Single Silk Fibers , 2008, Applied spectroscopy.

[37]  D. Lyman,et al.  Attenuated Total Reflection Fourier Transform Infrared Spectroscopy Analysis of Human Hair Fiber Structure , 2008, Applied spectroscopy.

[38]  Koichi Nishikida,et al.  Effective path length in attenuated total reflection spectroscopy. , 2008, Analytical chemistry.

[39]  L. Langenhove,et al.  FT-IR spectroscopy of spider and silkworm silks, part I : different sampling techniques , 2008 .

[40]  F. Kremer,et al.  Structure-property relationships in major ampullate spider silk as deduced from polarized FTIR spectroscopy , 2007, The European physical journal. E, Soft matter.

[41]  A. Barth.  Infrared spectroscopy of proteins. , 2007, Biochimica et biophysica acta.

[42]  Lisa J. Mauer,et al.  Differentiation of crude lipopolysaccharides from Escherichia coli strains using fourier transform infrared spectroscopy and chemometrics , 2006 .

[43]  B. Singh,et al.  A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods. , 2004, Biochemistry.

[44]  W. Hennink,et al.  Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. , 2001, Analytical biochemistry.

[45]  Brian C. Smith.  Fundamentals of Fourier Transform Infrared Spectroscopy , 1995 .

[46]  P. Haris,et al.  Protein secondary structure from Fourier transform infrared and/or circular dichroism spectra. , 1993, Analytical biochemistry.

[47]  F. Dousseau,et al.  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. , 1990, Biochemistry.

[48]  K. Esbensen,et al.  Principal component analysis , 1987 .

[49]  T. Matsui,et al.  A Study of the Amide III Band by FT-IR Spectrometry of the Secondary Structure of Albumin, Myoglobin, and γ-Globulin , 1987 .

[50]  H. Susi,et al.  Examination of the secondary structure of proteins by deconvolved FTIR spectra , 1986, Biopolymers.

[51]  E. Gratton,et al.  Correlation of IR spectroscopic, heat capacity, diamagnetic susceptibility and enzymatic measurements on lysozyme powder , 1980, Nature.

[52]  T. Hirschfeld.  Diagnosis and correction of wedging errors in absorbance subtract Fourier transform infrared spectrometry , 1979 .

[53]  G. Gouadec,et al.  Raman and IR micro-analysis of high performance polymer fibres tested in traction and compression , 2009 .

[54]  H. Mantsch,et al.  The use and misuse of FTIR spectroscopy in the determination of protein structure. , 1995, Critical reviews in biochemistry and molecular biology.

[55]  S. Venyaminov,et al.  Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. III. Estimation of the protein secondary structure , 1990, Biopolymers.

[56]  S. Venyaminov,et al.  Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands , 1990, Biopolymers.

[57]  S. Venyaminov,et al.  Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α‐, β‐, and random coil conformations , 1990, Biopolymers.