Results 31 to 40 of about 4,535,136 (383)
Exploiting Peptide Self-Assembly for the Development of Minimalistic Viral Mimetics
Frontiers in Chemistry, 2021 Viruses are natural supramolecular nanostructures that form spontaneously by molecular self-assembly of complex biomolecules. Peptide self-assembly is a versatile tool that allows mimicking viruses by creating their simplified versions through the design
Patrizia Janković +4 more
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Antioxidant Activities of Sorghum Kafirin Alcalase Hydrolysates and Membrane/Gel Filtrated Fractions
Antioxidants, 2019 Sorghum has a significant amount of proteins, especially kafirin; however, limited information is available on evaluating its potential for peptide antioxidants.
Shiwei Xu, Yanting Shen, Yonghui Li
doaj +1 more source
A Peptide Core Motif for Binding to Heterotrimeric G Protein α Subunits [PDF]
, 2005 Recently, in vitro selection using mRNA display was used to identify a novel peptide sequence that binds with high affinity to G{alpha}i1. The peptide was minimized to a 9-residue sequence (R6A-1) that retains high affinity and specificity for the GDP ...
Adhikari, Anirban +4 more
core +2 more sources
Molecules, 2012 Enzymatic proteolysis of food proteins is considered a promising method to generate antibacterial peptides. The objective of the present study was to isolate and characterize peptide fraction from the pepsin hydrolysate of half-fin anchovy (Setipinna ...
Dong-Feng Wang +3 more
doaj +1 more source
Solution to peptide sequencing challenge [PDF]
Analytical and Bioanalytical Chemistry, 2013 The cyclic peptide described is kalata B1 [1, 2] and its structure is shown in Fig. 1. The partial reduction of the cyclic peptide [2, 3] allows one to establish the disulfide connectivity. The first peptide is amino-ethylated at only {2}Cys and {5}Cys, whereas the second peptide is amino-ethylated at only {1}Cys and {4}Cys.
openaire +4 more sources
A Dynamic Programming Approach to De Novo Peptide Sequencing via Tandem Mass Spectrometry [PDF]
, 2001 The tandem mass spectrometry fragments a large number of molecules of the same peptide sequence into charged prefix and suffix subsequences, and then measures mass/charge ratios of these ions.
Chen, Ting +4 more
core +3 more sources
Self-assembly of minimal peptoid sequences [PDF]
, 2020 Peptoids are biofunctional N-substituted glycine peptidomimics. Their self-assembly is of fundamental interest because they demonstrate alternatives to conventional peptide structures based on backbone chirality and beta-sheet hydrogen bonding.
Castelletto, Valeria +8 more
core +2 more sources
Frontiers in Immunology, 2017 Several pathogenic bacteria are able to induce the attaching and effacing (A/E) lesion. The A/E lesion is caused by effector proteins, such as Escherichia coli-secreted protein B (EspB), responsible together with Escherichia coli-secreted protein D for ...
Roxane Maria Fontes Piazza +4 more
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The Carboxyl-Terminal Segment of Apolipoprotein A-V Undergoes a Lipid-Induced Conformational Change [PDF]
, 2010 Apolipoprotein (apo) A-V is a 343-residue, multidomain protein that plays an important role in regulation of plasma triglyceride homeostasis. Primary sequence analysis revealed a unique tetraproline sequence (Pro293-Pro296) near the carboxyl terminus of ...
Lee, B. L. +4 more
core +2 more sources
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry.
Proceedings of the National Academy of Sciences of the United States of America, 2004 Peptide sequence analysis using a combination of gas-phase ion/ion chemistry and tandem mass spectrometry (MS/MS) is demonstrated. Singly charged anthracene anions transfer an electron to multiply protonated peptides in a radio frequency quadrupole ...
J. Syka +4 more
semanticscholar +1 more source