scholarly journals Proline puckering parameters for collagen structure simulations

AIP Advances ◽  
2015 ◽  
Vol 5 (3) ◽  
pp. 037124 ◽  
Author(s):  
Di Wu
Keyword(s):  
Collagen Structure ◽  
Puckering Parameters

Can fractal dimension analysis be used in quantitating collagen structure?

2021 ◽  
Author(s):  
Feng Tian ◽  
Yuzhi Jiang ◽  
Yi Liu ◽  
Shuliang Lu ◽  
Jianfei Yang ◽  
...  
Keyword(s):  
Fractal Dimension ◽  
Collagen Structure ◽  
Dimension Analysis ◽  
Fractal Dimension Analysis

Normal Collagen Structure in the Posterior Ankle Capsule in Different Types of Clubfeet

1999 ◽  
Vol 8 (4) ◽  
pp. 261-263 ◽  
Author(s):  
Johannes Antonius van der Sluijs ◽  
Johannes Egbertus Henricus Pruys
Keyword(s):  
Collagen Structure ◽  
Different Types

scholarly journals Collagen heterogeneity within different growth regions of long bones of rachitic and nonrachitic chicks

1972 ◽  
Vol 127 (4) ◽  
pp. 715-720 ◽  
Author(s):  
Bryan P. Toole ◽  
Andrew H. Kang ◽  
Robert L. Trelstad ◽  
Jerome Gross
Keyword(s):  
Vitamin D ◽  
Amino Acid ◽  
Bone Matrix ◽  
Bone Collagen ◽  
Long Bone ◽  
Long Bones ◽  
Collagen Structure ◽  
Collagen Molecules ◽  
Relationship Of ◽  
Chain Type

The different anatomical regions involved in osteogenesis in the chick long bone have been examined for heterogeneities in collagen structure that might relate to the mechanism of ossification. Experimentally induced lathyrism was employed to enhance collagen solubility, and vitamin D deficiency to allow accumulation of osteoid, the precursor of bone matrix. The extractable lathyritic collagens of the cartilaginous and osseous regions of growing long bones from rachitic and non-rachitic chicks were examined for α-chain type and amino acid composition. In both groups of animals the growth plate and cartilaginous regions of the epiphysis gave collagen molecules of the constitution [α1(II)]3, whereas the ossifying regions contained [α1(I)]2 α2. The degree of hydroxylation of the lysine moieties was increased by approximately 50% in the α1(I)-chain and α2-chain of rachitic bone collagen. Since uncalcified osteoid is greatly enriched in rachitic bone, it is concluded that the collagen of osteoid has the configuration [α1(I)]2 α2, similar to that of bone matrix, but has an elevated hydroxylysine content. The possible relationship of this difference to the mechanism of calcification is discussed.

Methyl β-lactoside [methyl β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside] monohydrate: a solvomorphism study

2021 ◽  
Vol 77 (10) ◽  
pp. 668-674
Author(s):  
Jieye Lin ◽  
Allen G. Oliver ◽  
Anthony S. Serianni
Keyword(s):  
Hydrogen Bonds ◽  
Visual Inspection ◽  
Crystalline Lattice ◽  
Glycosidic Linkage ◽  
Spontaneous Transformation ◽  
Air Drying ◽  
Hydroxymethyl Group ◽  
Boat Form ◽  
Puckering Parameters ◽  
Twist Boat

Methyl β-lactoside [methyl β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside] monohydrate, C13H24O11·H2O, (I), was obtained via spontaneous transformation of methyl β-lactoside methanol solvate, (II), during air-drying. Cremer–Pople puckering parameters indicate that the β-D-Galp (β-D-galactopyranosyl) and β-D-Glcp (β-D-glucopyranosyl) rings in (I) adopt slightly distorted 4 C 1 chair conformations, with the former distorted towards a boat form (B C1,C4) and the latter towards a twist-boat form (O5 S C2). Puckering parameters for (I) and (II) indicate that the conformation of the βGalp ring is slightly more affected than the βGlcp ring by the solvomorphism. Conformations of the terminal O-glycosidic linkages in (I) and (II) are virtually identical, whereas those of the internal O-glycosidic linkage show torsion-angle changes of 6° in both C—O bonds. The exocyclic hydroxymethyl group in the βGalp residue adopts a gt conformation (C4′ anti to O6′) in both (I) and (II), whereas that in the βGlcp residue adopts a gg (gauche–gauche) conformation (H5 anti to O6) in (II) and a gt (gauche–trans) conformation (C4 anti to O6) in (I). The latter conformational change is critical to the solvomorphism in that it allows water to participate in three hydrogen bonds in (I) as opposed to only two hydrogen bonds in (II), potentially producing a more energetically stable structure for (I) than for (II). Visual inspection of the crystalline lattice of (II) reveals channels in which methanol solvent resides and through which solvent might exchange during solvomorphism. These channels are less apparent in the crystalline lattice of (I).

Comparative Analysis of the Proteomic Profile of Cattle Hides that Produce Loose and Tight Leather using In-Gel Tryptic Digestion followed by LC-MS/MS

2020 ◽  
Vol 115 (11) ◽  
pp. 399-408
Author(s):  
Catherine Maidment ◽  
Meekyung Ahn ◽  
Rafea Naffa ◽  
Trevor Loo ◽  
Gillian Norris
Keyword(s):  
Type I Collagen ◽  
Raw Material ◽  
Type I ◽  
Collagen Structure ◽  
Proteomic Profile ◽  
Collagen Network ◽  
Collagen Concentration ◽  
Different Types ◽  
Molecular Components ◽  
First Time

Looseness is a defect found in leather that reduces its quality by causing a wrinkly appearance in the finished product, resulting in a reduction in its value. Earlier studies on loose leather using microscopy and Raman spectroscopy reported a change in the collagen structure of loose leather. In this study, proteomics was used to investigate the possible molecular causes of looseness in the raw material, the first time such a study has been carried out. Proteins extracted from two regions of raw hide using two different methods were analysed; those taken from the distal axilla, an area prone to looseness, and those taken from the backbone which is less prone to looseness. Analyses using 1DE-LC-MS/MS showed that although the overall collagen concentration was similar in both areas of the hide, the distribution of the different types of collagen differed.  Specifically, concentrations of type I collagen, and the collagen-associated proteoglycan decorin were lower in samples taken from the distal axilla, symptomatic of a collagen network with excess space seen for these samples using confocal microscopy. This study suggests a possible link between the molecular components of raw cattle hide and looseness and more importantly between the molecular components of skin and skin defects. There is therefore potential to develop biomarkers for looseness which will enable early preventative action.

Development of a tannic acid cross-linking process for obtaining 3D porous cell-laden collagen structure

2018 ◽  
Vol 110 ◽  
pp. 497-503 ◽  
Author(s):  
JiUn Lee ◽  
Miji Yeo ◽  
WonJin Kim ◽  
YoungWon Koo ◽  
Geun Hyung Kim
Keyword(s):  
Tannic Acid ◽  
Cross Linking ◽  
Collagen Structure

scholarly journals The use of Dermacell® in Fingertip Injury

2019 ◽  
Vol 1 (2) ◽  
pp. 14-22 ◽  
Author(s):  
Wu, Tsung-Hsuan ◽  
Giampietro Bertasi
Keyword(s):  
Immune Response ◽  
Collagen Scaffold ◽  
Tissue Scaffolds ◽  
Cellular Growth ◽  
Collagen Structure ◽  
Tissue Remodelling ◽  
Fingertip Injury ◽  
Viable Cells ◽  
Native Collagen ◽  
Immunogenic Response

Matrices or tissue scaffolds provide a collagen structure for tissue remodelling while the removal of viable cells aims to minimize or prevent inflammatory or immunogenic response. Allograft collagen scaffold can support the patient’s own cellular ingrowth, ingeneered to minimize an immune response and to yeld a bio-compatible matrix and support incoming cellular growth. The decellyularized dermis retains its growth factors, native collagen scaffold, and elastin, thanks to a LifeNet Health proprietaryprocessin technology.

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