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Journal ArticleDOI

Conformation transition kinetics of regenerated Bombyx mori silk fibroin membrane monitored by time-resolved FTIR spectroscopy

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TLDR
The ethanol-induced conformation transition of regenerated Bombyx mori silk fibroin membrane from a poorly defined to the well ordered state was monitored by time-resolved Fourier transform infrared spectroscopy (FTIR) for the first time.
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This article is published in Biophysical Chemistry.The article was published on 2001-01-31. It has received 267 citations till now. The article focuses on the topics: Infrared spectroscopy & Fibroin.

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Citations
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Journal ArticleDOI

Determining Beta-Sheet Crystallinity in Fibrous Proteins by Thermal Analysis and Infrared Spectroscopy

TL;DR: In this paper, B. mori silk fibroin films were studied thermally using temperature-modulated differential scanning calorimetry (TMDSC) to obtain the reversing heat capacity.
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Water‐Stable Silk Films with Reduced β‐Sheet Content

TL;DR: The preparation of water‐stable films from regenerated silk fibroin solutions, with reduced β‐sheet content, which support human adult stem‐cell expansion in vitro in a similar or improved fashion to the crystallized proteins in film form.
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Dynamic Protein−Water Relationships during β-Sheet Formation

TL;DR: In this article, the polymer−water interaction in a model fibrous protein was investigated, and the detailed structural changes of silk fibroin during heating and during isothermal crystallization above the glass transition temperature was analyzed.
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Regeneration of Bombyx mori silk by electrospinning. Part 3: characterization of electrospun nonwoven mat

TL;DR: In this paper, a regenerated Bombyx mori silk fibroin in formic acid was electrospun and the morphological, chemical and mechanical properties of these nanofibers were examined by field emission environmental scanning electron microscopy (FESEM), Raman spectroscopy (RS), Fourier transform infrared (FTIR), X-ray diffraction (XRD), and tensile testing.
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Synchrotron FTIR microspectroscopy of single natural silk fibers.

TL;DR: For the first time, from S-FTIR the β-sheet content in a range of natural single silk fibers is determined, 28 ± 4, 23 ± 2, and 17 ± 4% in Bombyx mori, Antheraea pernyi, and Nephila edulis silks, respectively.
References
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Journal ArticleDOI

Protein secondary structures in water from second-derivative amide I infrared spectra.

TL;DR: A method of analysis of second-derivative amide I spectra whereby the frequencies of bands due to different secondary structures can be obtained is demonstrated and the band intensities obtained provide a useful method for estimating the relative amounts of different structures.
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Protein Folding: A Perspective from Theory and Experiment.

TL;DR: This review presents the progess made recently in understanding key elements of this reaction and describes a solution to the often quoted Levinthal Paradox.
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Fast events in protein folding: helix melting and formation in a small peptide.

TL;DR: The observation of the fast kinetics of helix melting in a small 21-residue alanine-based peptide demonstrates that secondary structure formation is fast enough to be a key event at early times in the protein-folding process and that helices are capable of forming before long range tertiary contacts are made.
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