ChemInform Abstract: Recent Developments in Kainoid Amino Acid Chemistry

ChemInform ◽  
2010 ◽  
Vol 27 (28) ◽  
pp. no-no
Author(s):  
A. F. PARSONS
Keyword(s):  
Amino Acid ◽  
Recent Developments

Recent developments in kainoid amino acid chemistry

Tetrahedron ◽  
1996 ◽  
Vol 52 (12) ◽  
pp. 4149-4174 ◽  
Author(s):  
Andrew F Parsons
Keyword(s):  
Amino Acid ◽  
Recent Developments

Recent Advances in the Feeding and Nutrition of Aphids

1964 ◽  
Vol 96 (1-2) ◽  
pp. 241-249 ◽  
Author(s):  
J. L. Auclair
Keyword(s):  
Amino Acid ◽  
Digestive Enzymes ◽  
Host Plants ◽  
Artificial Feeding ◽  
Pea Aphid ◽  
Nutritional Requirements ◽  
Feeding Method ◽  
Recent Developments ◽  
Aphid Feeding ◽  
Successive Generations

AbstractSome recent developments on aphid digestive enzymes, aphid feeding and nutrition on host-plants, and on artificial media are briefly reviewed. A chemically defined diet, on which pea aphid life and reproduction can be sustained during two successive generations, is described. An important feature of this successful chemical diet concerns its amino acid composition, which was based on that of pea aphid blood and honeydew. An artificial feeding method for aphids divorced from their host-plants should prove a valuable tool in the study of the nutritional requirements and the intermediary metabolism of these insects, as well as in determining the influence of dietary constituents on polymorphism and in relation to the phenomena of plant resistance to aphids.

Recent progress in the field of neoglycoconjugate chemistry

2010 ◽  
Vol 1 (1) ◽  
pp. 85-96
Author(s):  
Carmen Jiménez-Castells ◽  
Sira Defaus ◽  
David Andreu ◽  
Ricardo Gutiérrez-Gallego
Keyword(s):  
Amino Acid ◽  
Recent Progress ◽  
Heterogeneous Mixture ◽  
Naturally Occurring ◽  
Single Protein ◽  
Recent Developments

AbstractGlycosylation is probably the most complex secondary gene event that affects the vast majority of proteins in nature resulting in the occurrence of a heterogeneous mixture of glycoforms for a single protein. Many functions are exerted by single monosaccharides, well-defined oligosaccharides, or larger glycans present in these glycoproteins. To unravel these functions it is of the utmost importance to prepare well-defined single glycans conjugated to the underlying aglycon. In this review, the most recent developments are described to address the preparation of carbohydrate-amino acid (glyco-conjugates). Naturally occurring N- and O-linked glycosylation are described and the preparation of non-natural sugar-amino acid linkages are also included.

Expanding the genetic code of mammalian cells

2017 ◽  
Vol 45 (2) ◽  
pp. 555-562 ◽  
Author(s):  
James S. Italia ◽  
Yunan Zheng ◽  
Rachel E. Kelemen ◽  
Sarah B. Erickson ◽  
Partha S. Addy ◽  
...  
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Mammalian Cells ◽  
Living Cells ◽  
Structure And Function ◽  
Unnatural Amino Acid ◽  
Full Potential ◽  
Recent Developments ◽  
Small Footprint ◽  
And Function

In the last two decades, unnatural amino acid (UAA) mutagenesis has emerged as a powerful new method to probe and engineer protein structure and function. This technology enables precise incorporation of a rapidly expanding repertoire of UAAs into predefined sites of a target protein expressed in living cells. Owing to the small footprint of these genetically encoded UAAs and the large variety of enabling functionalities they offer, this technology has tremendous potential for deciphering the delicate and complex biology of the mammalian cells. Over the last few years, exciting progress has been made toward expanding the toolbox of genetically encoded UAAs in mammalian cells, improving the efficiency of their incorporation and developing innovative applications. Here, we provide our perspective on these recent developments and highlight the current challenges that must be overcome to realize the full potential of this technology.

scholarly journals Leri: a web-server for identifying protein functional networks from evolutionary couplings

2020 ◽  
Author(s):  
Ngaam J. Cheung ◽  
Arun T. John Peter ◽  
Benoit Kornmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Function ◽  
Structure Prediction ◽  
High Performance ◽  
Web Server ◽  
Functional Networks ◽  
Computational Results ◽  
High Quality ◽  
Recent Developments

ABSTRACTInformation on the co-evolution of amino acid pairs in a protein can be used for endeavors such as protein engineering, mutation design, and structure prediction. Here we report a method that captures significant determinants of proteins using estimated co-evolution information to identify networks of residues, termed “residue communities”, relevant to protein function. By taking advantage of recent developments in high-performance and parallel computing, we constructed a web-server, Leri, that identifies relevant residue communities to allow researchers to investigate how a protein evolves and folds for function(s). All the data of the computational results including high-quality images can be downloaded and presented for publication. This web-server, written in C++, is sufficiently rapid to enable the studies on proteins of up to 400 amino acids.

Tryptophan oxygenation: mechanistic considerations

2012 ◽  
Vol 40 (3) ◽  
pp. 509-514 ◽  
Author(s):  
James H. Naismith
Keyword(s):  
Natural Products ◽  
Amino Acid ◽  
Molecular Oxygen ◽  
Ring System ◽  
Hydrophobic Core ◽  
Indole Ring ◽  
Multiple Strategies ◽  
Tryptophan Dioxygenase ◽  
Recent Developments ◽  
Hydrophobic Anchor

From a protein structural viewpoint, tryptophan is often considered an inert structural amino acid, playing a role as a hydrophobic anchor in membrane proteins or as part of the hydrophobic core of soluble proteins. However, tryptophan is the only polyaromatic amino acid and, from a chemical viewpoint, possesses unique reactivity owing to the electron-richness of the indole system. This reactivity is seen in the area of natural products and metabolites which have exquisite modifications of the indole ring system. Enzymes have evolved multiple strategies to break or modify the indole ring; one particular class is the IDO/TDO (indoleamine/tryptophan dioxygenase) superfamily. A new member of this family, PrnB, on the surface catalyses a very different reaction, but actually shares much of the early chemistry with the tryptophan dioxygenases. Studies on PrnB have contributed to our understanding of the wider superfamily. In the present mini-review, recent developments in our understanding of how the TDO class of enzymes use activated molecular oxygen to break the indole ring are discussed.

scholarly journals Exploring amino acid functions in a deep mutational landscape

2020 ◽  
Author(s):  
Alistair Dunham ◽  
Pedro Beltrao
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Clustering Analysis ◽  
Chemical Properties ◽  
Diverse Range ◽  
Mutational Landscape ◽  
Charged Amino Acids ◽  
Large Numbers ◽  
Recent Developments ◽  
And Chemical Properties

AbstractAmino acids fulfil a diverse range of roles in proteins, each utilising its chemical properties in different ways in different contexts to create required functions. For example, cysteines form disulphide or hydrogen bonds in different circumstances and charged amino acids do not always make use of their charge. The repertoire of amino acid functions and the frequency at which they occur in proteins remains understudied. Measuring large numbers of mutational consequences, which can elucidate the role an amino acid plays, was prohibitively time consuming until recent developments in deep mutational scanning. In this study we gathered data from 28 deep mutational scanning studies, covering 6291 positions in 30 proteins, and used the consequences of mutation at each position to define a mutational landscape. We demonstrated rich relationships between this landscape and biophysical or evolutionary properties. Finally, we identified 100 functional amino acid subtypes with a data-driven clustering analysis and studied their features, including their frequencies and chemical properties such as tolerating polarity, hydrophobicity or being intolerant of charge or specific amino acids. The mutational landscape and amino acid subtypes provide a foundational catalogue of amino acid functional diversity, which will be refined as the number of studied protein positions increases.

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