THE DEPENDENCE OF THE CONFORMATIONS OF SYNTHETIC POLYPEPTIDES ON AMINO ACID COMPOSITION<sup>1,2</sup>

Blout, E. R.; Loze, C. de; Bloom, S. M.; Fasman, G. D.

doi:10.1021/ja01499a080

Cited by 194 publications

(61 citation statements)

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“…It has been reported from amino acid analysis that human cuticle cells contain a higher percentage of amino acids that are not usually found in α-helical peptides. 15,16 Further examination of these spectra was conducted using second derivative spectra as displayed in Fig. 1(d).…”

Section: Results and Discussion 31 Ir Spectral Imaging Of Chemical mentioning

confidence: 99%

Measuring changes in chemistry, composition, and molecular structure within hair fibers by infrared and Raman spectroscopic imaging

2011

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Abstract. Spatially resolved infrared (IR) and Raman images are acquired from human hair cross sections or intact hair fibers. The full informational content of these spectra are spatially correlated to hair chemistry, anatomy, and structural organization through univariate and multivariate data analysis. Specific IR and Raman images from untreated human hair describing the spatial dependence of lipid and protein distribution, protein secondary structure, lipid chain conformational order, and distribution of disulfide cross-links in hair protein are presented in this study. Factor analysis of the image plane acquired with IR microscopy in hair sections, permits delineation of specific micro-regions within the hair. These data indicate that both IR and Raman imaging of molecular structural changes in a specific region of hair will prove to be valuable tools in the understanding of hair structure, physiology, and the effect of various stresses upon its integrity. C 2011 Society of Photo-Optical Instrumentation Engineers (SPIE).

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Section: Results and Discussion 31 Ir Spectral Imaging Of Chemical mentioning

confidence: 99%

Measuring changes in chemistry, composition, and molecular structure within hair fibers by infrared and Raman spectroscopic imaging

2011

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“…One might therefore expect that the cuticle would be richer than the cortex (or the parent fibre) in those amino acids which have difficulty in forming an iX-helix and correspondingly poorer in those amino acids which readily form an iX-helix. A classification has been made of amino acids according to their ability to produce synthetic polypeptides which have an iX-helical structure in the solid state and in solution (Blout et al 1960;Blout 1962). When one compares this classification with Table 6, it is found that all those amino acids which are enriched in the cuticle are non iX-helix-forming according to Blout (1962), with the exception of glycine which is unclassified.…”

Section: Examination Of the Values Inmentioning

confidence: 99%

The Chemical Composition of Wool II. Analysis of the Major Histological Components Produced by Ultrasonic Disintegration

Jh¹,

Gv²,

Nl³

1965

Aust. Jnl. Of Bio. Sci.

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SummaryUltrasonic disruption of powdered Merino wool in formic acid and dichloroacetic acid causes some protein to be dissolved, but the amino acid content of the residual wool is unchanged by the treatment. Cortical cells and disrupted cortical cells are found to have the same composition as the parent fibre, which is to be expected because the latter consists of about 90 % cortical cells. However, the cuticle of Merino wool is different in composition from the parent fibre, being richer in cysteic acid, serine, proline, glycine, valine, and cystine, and poorer in aspartic acid, threonine, glutamic acid, methionine, isoleucine, leucine, tyrosine, phenylalanine, and arginine than the whole fibre. Thus the cuticle is considerably less polar than the fibre as a whole. With the exceptions detailed below, it is found that the first group of amino acids listed above are classified as non a.helix.forming and the second group as a·helix· forming by Blout (1962). The exceptions are isoleucine and threonine, whilst arginine and glycine are not classified. It is therefore postulated that the cuticle is amorphous because of its high content of non a·helix.forming amino acids. The cuticle of Lincoln wool shows similar differences to those already given for Merino cuticle but, in addition, contains less lysine and histidine than the whole fibre.

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“…However, the samples used in these studies were mixtures of the various native sericin proteins, therefore the structure of the individual proteins is unknown and the contribution of specific sequences toward secondary structure is not confirmed. Sericin model peptides such as poly(L-serine) (11-16), poly(O-benzyl-L-serine) (12), and poly(O-acetyl-L-serine) (13,14) were synthesized for structural feature characterization. The ability of poly(L-serine) to fold into a ␤ conformation depended on molecular weight.…”

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Cloning, Expression, and Assembly of Sericin-like Protein

Huang

Valluzzi

Bini

et al. 2003

Journal of Biological Chemistry

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Recombinant sericin proteins of different molecular masses (17.4, 31.9, and 46.5 kDa), based on the 38-amino acid repetitive motif of native sericin, were cloned, expressed, and purified. The recombinant sericin self-assembled during dialysis (starting concentration of 2.5 mg/ml) forming twisted fibers. Circular dichroism and Fourier transform infrared spectroscopy studies demonstrated protein conformational transitions occurred from random coil to ␤-sheets during the dialysis. Congo red-stained recombinant sericin fibrils exhibited applegreen birefringence, indicating long-range order in the array of ␤-sheets. Biosynthetic sericin has a high content of polar amino acids (e.g. Silk of Bombyx mori is composed of two kinds of proteins: the fibroin which is synthesized in the posterior silk gland and the sericins produced by the middle silk gland. The sericins bind two fibroin fibers together in the anterior region of the gland as the fibers are spun to form the cocoon. Sericins represent a family of proteins whose molecular mass ranges from 20 to 310 kDa (2, 3) and are characterized by an unusually high serine content, 38.1 mol % (4). Sericins are soluble in hot water, which makes it possible to degum the silk fibroin threads.Two genes encode sericins, Ser1 and Ser2 (5-8). The different molecular weight sericins are the products of different splicing events at the transcript level. Some conformation studies with sericins from the silk gland of B. mori or regenerated sericin from B. mori cocoons suggested random coil with some ␤ structure (9, 10). However, the samples used in these studies were mixtures of the various native sericin proteins, therefore the structure of the individual proteins is unknown and the contribution of specific sequences toward secondary structure is not confirmed. Sericin model peptides such as poly(L-serine) (11-16), poly(O-benzyl-L-serine) (12), and poly(O-acetyl-L-serine) (13,14) were synthesized for structural feature characterization. The ability of poly(L-serine) to fold into a ␤ conformation depended on molecular weight. Low molecular weight poly(L-serine) (molecular weight 650) was soluble and adopted a random coil conformation in aqueous solution, whereas high molecular weight poly(L-serine) (molecular weight 105,000) formed ␤-sheets and was insoluble in water (11). However, homopolypeptides like poly(L-serine) do not match native sericin in terms of amino acid composition, sequence, and molecular weight. Therefore, to better understand sericin structure, interactions between sericin and fibroin, and the biological relevance of sericin in fiber structure, high molecular weight pure sericin-like proteins are required.Sericin 1 encoded by Ser 1 consists of 70 repeats of the 38-amino acid motif (5): SSTGSSSNTDSNSNSVGSSTS-GGSSTYGYSSNSRDGSV. The molecular mass of sericin 1 proteins is 76 -284 kDa. The 38-amino acid repeat motif exhibits a high content of hydrophilic amino acids: 44.7% serine, 10.5% threonine, and 7.9% tyrosine, very close to the average amino acid composition of serici...

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THE DEPENDENCE OF THE CONFORMATIONS OF SYNTHETIC POLYPEPTIDES ON AMINO ACID COMPOSITION^1,2

Cited by 194 publications

References 1 publication

Measuring changes in chemistry, composition, and molecular structure within hair fibers by infrared and Raman spectroscopic imaging

Measuring changes in chemistry, composition, and molecular structure within hair fibers by infrared and Raman spectroscopic imaging

The Chemical Composition of Wool II. Analysis of the Major Histological Components Produced by Ultrasonic Disintegration

Cloning, Expression, and Assembly of Sericin-like Protein

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THE DEPENDENCE OF THE CONFORMATIONS OF SYNTHETIC POLYPEPTIDES ON AMINO ACID COMPOSITION1,2

Cited by 194 publications

References 1 publication

Measuring changes in chemistry, composition, and molecular structure within hair fibers by infrared and Raman spectroscopic imaging

Measuring changes in chemistry, composition, and molecular structure within hair fibers by infrared and Raman spectroscopic imaging

The Chemical Composition of Wool II. Analysis of the Major Histological Components Produced by Ultrasonic Disintegration

Cloning, Expression, and Assembly of Sericin-like Protein

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Product

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THE DEPENDENCE OF THE CONFORMATIONS OF SYNTHETIC POLYPEPTIDES ON AMINO ACID COMPOSITION^1,2