Zobrazeno 1 - 10
of 119
pro vyhledávání: '"DSSP (hydrogen bond estimation algorithm)"'
Amino acid side chain contribution to protein FTIR spectra: impact on secondary structure evaluation
Autor:
Erik Goormaghtigh, Joëlle De Meutter
Publikováno v:
European Biophysics Journal
Prediction of protein secondary structure from FTIR spectra usually relies on the absorbance in the amide I–amide II regionof the spectrum. It assumes that the absorbance in this spectral region, i.e., roughly 1700–1500 cm−1 is solely arising f
Publikováno v:
Human Mutation, 42, 7, pp. 799-810
Human Mutation
Human Mutation, 42, 799-810
Human Mutation
Human Mutation, 42, 799-810
Hereditary disorders are frequently caused by genetic variants that affect pre‐messenger RNA splicing. Though genetic variants in the canonical splice motifs are almost always disrupting splicing, the pathogenicity of variants in the noncanonical s
Autor:
Weiwei Xue, Xianquan Ming, Haiqing Zhan, Feng Zhan, Rong Huang, Hongyan Yu, Gao Tu, Jing Jing
Publikováno v:
Physical Chemistry Chemical Physics. 23:11717-11726
Tau misfolding plays a significant role in some neurodegenerative diseases such as Alzheimer's disease (AD). It is intrinsically disordered and highly soluble under normal physiological conditions. While the protein will aggregate to form paired heli
Publikováno v:
Restaurant and hotel consulting. Innovations. 3:237-251
The topicality. Serious changes in the structure of nutrition associated with changes in lifestyle, a decrease in energy consumption, lead to the fact that none of the population groups receives from the food consumed the amount of essential nutrient
Autor:
Erik Goormaghtigh, Joëlle De Meutter
Publikováno v:
Analytical Chemistry. 93:1561-1568
Obtaining protein secondary structure content from high-resolutionstructures requires definitions and thresholds for the various parameters involved, typicallyhydrogen bond energy or length/angle and backbone φ/ψ angles. Several definitions arecurr
Publikováno v:
The Protein Journal. 39:308-317
Surface accessibility of different types of the same elements of secondary structure has been studied in 10 non-redundant sets of proteins (total number of three-dimensional structures is 1730) with a help of DSSP (Dictionary of Secondary Structure o
Autor:
Joëlle De Meutter, Erik Goormaghtigh
Publikováno v:
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 18, Iss, Pp 1864-1876 (2020)
Computational and Structural Biotechnology Journal, 18
Computational and Structural Biotechnology Journal, Vol 18, Iss, Pp 1864-1876 (2020)
Computational and Structural Biotechnology Journal, 18
While several Raman, CD or FTIR spectral libraries are available for well-characterized proteins of known structure, proteins themselves are usually very difficult to acquire, preventing a convenient calibration of new instruments and new recording m
Autor:
Nikita Jain, S. Udhaya Kumar, Prangya Paramita Jena, Siva Ramamoorthy, Hatem Zayed, C. George Priya Doss, D Thirumal Kumar
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 39:1795-1810
Krabbe disease (KD), also known as globoid cell leukodystrophy disease, is an autosomal recessive lysosomal storage genetic disorder, which is caused by the deficiency of galactocerebrosidase (GALC) coding gene (GALC). This study aimed to use extensi
Autor:
Chen Keasar, Tomer Sidi
Publikováno v:
Bioinformatics. 36:3733-3738
Motivation The Protein Data Bank (PDB), the ultimate source for data in structural biology, is inherently imbalanced. To alleviate biases, virtually all structural biology studies use nonredundant (NR) subsets of the PDB, which include only a fractio
The development of AlphaFold2 was a paradigm-shift in the structural biology community; herein we assess the ability of AlphaFold2 to predict disordered regions against traditional sequence-based disorder predictors. We find that a näaive use of Dic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5cc550547372d72650ab41879d53133c
https://doi.org/10.1101/2021.09.27.461910
https://doi.org/10.1101/2021.09.27.461910