Refined molecular and crystal structure of silk I based on Ala-Gly and (Ala-Gly)2?Ser-Gly peptide sequence

Okuyama, Kenji; Somashekar, R.; Noguchi, Keiichi; Ichimura, Syuji

doi:10.1002/1097-0282(20011015)59:5<310::aid-bip1028>3.0.co;2-5

Cited by 42 publications

(12 citation statements)

References 47 publications

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“…In fact, a similar paracrystalline type of broadening was observed during the investigations of silk I. 6 In this article, we report the percentage of lattice distortion along different directions in the fiber by using Warren's Fourier method, 14,15 and hence, a procedure has been given to estimate the strain tensor components of silk I modi-fication. Also, the shape of the crystallite in silk I has been computed by using these results.…”

Section: Introductionsupporting

confidence: 61%

“…Silk III modification is observed in air-water interface of silk fibroin solution. 4 The crystal and molecular structure of silk II are given by Marsh et al, 5 and the structure of silk III was given by Valluzzi et al 4 Recently, refined molecular and crystal structure of silk I based on dipeptide and hexapeptide were reported by Okuyama et al 6 The broadening of X-ray reflection profiles in spun silk (II) fibers in terms of crystal size and strain have been studied extensively [7][8][9][10][11][12][13] by using Hosemann's one-dimensional paracrystalline model. In fact, a similar paracrystalline type of broadening was observed during the investigations of silk I.…”

Section: Introductionmentioning

confidence: 99%

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Strain–tensor components, crystallite shape, and their effects on crystalline structure in silk I

Sangappa

Okuyama

Somashekar

2004

J of Applied Polymer Sci

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By using the X-ray powder data obtained from Bombyx mori silk fibroin in silk I modification, we have estimated the strains by using profiles of several (hkl ) reflections observed in the fibroin. For this purpose, we have used line profile simulation and matching with the experimental, on the basis of a paracrystalline one-dimensional Hosemann's model proposed earlier. The shape of the crystallite and size along different directions in the fibroin have also been estimated and presented here. From these results, the strain tensor has been computed by using the approach given by Wilke and Martis. The effect of these strains on the molecular arrangement within the crystal structure and the nature of changes in the chain within the unit cell which participates in inducing the intrinsic strain during the formation of the fiber (silkII) are reported here. © 2004 Wiley Periodicals, Inc. J Appl Polym Sci 91: 3045-3053, 2004

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Section: Introductionsupporting

confidence: 61%

Section: Introductionmentioning

confidence: 99%

Strain–tensor components, crystallite shape, and their effects on crystalline structure in silk I

Sangappa

Okuyama

Somashekar

2004

J of Applied Polymer Sci

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“…2B, C) from 4.4 to 4.3 Å, indicating a shift from silk I to silk II structure. For comparison with our data, representative silk I and silk II model structures that had been taken by X-ray and electron diffraction, infrared spectroscopy, nuclear magnetic resonance, and raman spectroscopy were collected from literature [19][20][21][22][23][24][25][26][27][28][29][30] and resulted in three predictions of silk I structure models, the Crankshaft model [26], the out-of-register model [23] and the repeated β-turn type II model [20]. Silk II structure is commonly described by antiparallel β-sheets [31,32].…”

Section: Surface Characterization and Physicochemical Analysis Of Silmentioning

confidence: 99%

Silk fibroin as an organic polymer for controlled drug delivery

Hofmann

Foo

Rossetti

et al. 2006

Journal of Controlled Release

341

245

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“…Glycine and alanine mono-, di-, and tripeptides have been studied by quantum-chemical methods [10,11,15,16]. Theoretical methods can gain insight into special features and possible schemes of interaction with solvent molecules.…”

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confidence: 99%

10.1007/s11176-008-1024-z

2010

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Complex formation of scleroprotein models with an N-methylmorpholine N-oxide solvent was studied by the semiempirical PM3 method.Scleroproteins include a large group of fibrous proteins abundant in animal tissues: silk fibroin, fur and feather keratins, connective tissue collagen and elastin, and marine sponge and coral spongin. Since these proteins are fiber and film-forming, interest in their reprocessing by dissolution with the aim to obtain various items for medicine and biotechnology is constantly growing [135]. Search for new solvents and processing technologies for these natural polymers with unique properties is impossible without understanding of their structural features and mechanism of dissolution. Modern methods of computer simulation play special role in studying dissolution processes. Their results help to explain experimentally obtained regularities and predict the behavior of polymers upon dissolution. The aim of this work was to study the mechanism of dissolution of models of scleroprotein crystal structure by a quantumchemical method.

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Refined molecular and crystal structure of silk I based on Ala-Gly and (Ala-Gly)2?Ser-Gly peptide sequence

Cited by 42 publications

References 47 publications

Strain–tensor components, crystallite shape, and their effects on crystalline structure in silk I

Strain–tensor components, crystallite shape, and their effects on crystalline structure in silk I

Silk fibroin as an organic polymer for controlled drug delivery

10.1007/s11176-008-1024-z

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