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Effects of tissue hydration on nanoscale structural morphology and mechanics of individual Type I collagen fibrils in the Brtl mouse model of Osteogenesis Imperfecta
AFM Ultrastructure Genotype/phenotype D-periodic spacing Modulus Energy
2014/11/6
Type I collagen is the most abundant protein in mammals, and is a vital part of the extracellular matrix for numerous tissues. Despite collagen’s importance, little is known about its nanoscale morpho...
Nanoscale Structure of Type I Collagen Fibrils: Quantitative Measurement of D-spacing
Collagen fibril D-spacing 2D FFT AFM
2014/11/6
This article details a quantitative method to measure the D-periodic spacing of type I collagen fibrils using atomic force microscopy coupled with analysis using a two-dimensional fast fourier transfo...
Atomic-resolution structures of prion AGAAAAGA amyloid fibrils
Amyloid Fibrils Prion AGAAAAGA Palindrome Atomic-resolution Structures
2011/8/31
To the best of the authors knowledge, there is little structural data available on the AGAAAAGA palindrome in the hydrophobic region (113-120) of prion proteins due to the unstable, noncrystalline and...
Optimal atomic-resolution structures of prion AGAAAAGA amyloid fibrils
Optimal atomic-resolution structures prion AGAAAAGA amyloid fibrils
2011/1/5
To date, there is little structural data available on the AGAAAAGA palindrome in the hydrophobic region (113-120) of prion proteins, although many experimental studies have shown that this region has ...
In vitro formation and thermal transition of novel hybrid fibrils from type I fish scale collagen and type I porcine collagen
In vitro formation thermal transition novel hybrid fibrils type I fish scale collagen type I porcine collagen
2010/10/12
Novel type I collagen hybrid fibrils were fabricated by neutralizing a mixture of type I fish scale collagen solution and type I porcine collagen solution with a phosphate buffer saline at 28 °C. Thei...