Exploring the structure and stability of amino acids and glycine peptides in biocompatible ionic liquids

RSC Advances ◽  
2016 ◽  
Vol 6 (23) ◽  
pp. 18763-18777 ◽  
Author(s):  
Awanish Kumar ◽  
Meena Bisht ◽  
Pannuru Venkatesu
Keyword(s):  
Amino Acids ◽  
Ionic Liquids ◽  
Protein Structure ◽  
Biological Systems ◽  
Covalent Bonds ◽  
Peptide Bonds ◽  
Structure And Stability ◽  
Glycine Peptides

Amino acids (AAs) are vital components for a variety of biological systems and can be linked through covalent bonds (or peptide bonds) to form a protein structure.

scholarly journals Synthesis, extraction and idetification of meat bioactive peptides: a review

2021 ◽  
Vol 888 (1) ◽  
pp. 012058
Author(s):  
Edy Susanto ◽  
Anik Fadlilah ◽  
Muhammad Fathul Amin
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Functional Food ◽  
Bioactive Peptides ◽  
Peptide Identification ◽  
Bioactive Peptide ◽  
Covalent Bonds ◽  
Peptide Bonds ◽  
Body Location ◽  
Potential Use

Abstract The consumption of meat should consider the concept of functional food. The meat had a highquality protein and contain of bioactive peptide compounds. Amino acid was component of bioactive peptides compound. It joined by covalent bonds known as amide or peptide bonds. A lot of research was currently focused on the bioactive peptide compounds isolated from myofibril and sarcoplasmic proteins with the synthesis, extraction, and identification methods. This study used a systematic review to get the structure of amino acids that the source of bioactive components and the principle of synthesis, extraction and identification of bioactive peptide in the meat. This paper highlights were finding on the structure of amino acid in the meat. The proportion of amino acids was also different in each animal body location. The result identified that more than 170 peptides were released from the main structure of the myofibril (actin, myosin) and sarcoplasmic muscle proteins, and the synthesis, extraction and bioactive peptide identification in the meat as well as their potential use as functional food.

Principles of protein structure

Hemoglobin ◽  
2018 ◽  
pp. 1-10
Author(s):  
Jay F. Storz
Keyword(s):  
Amino Acids ◽  
Protein Structure ◽  
Functional Properties ◽  
Three Dimensional ◽  
Physiological Role ◽  
Dimensional Structure ◽  
Covalent Bonds ◽  
Base Camp

Chapter 1 reviews basic principles of protein structure—the nature of proteins as polymers of amino acids, the variety of amino acids, and the way in which the physicochemical properties of amino acid side chains influence the folding of a polymer into a three-dimensional protein with specific functional properties. Whereas the main chain polypeptide is linked together by covalent bonds, the three-dimensional structure of native state proteins is mainly stabilized by a multitude of noncovalent, weakly polar interactions. After securing the base camp with this brief overview of protein structure, the subsequent chapters explore the functional properties of hemoglobin, the biophysical mechanisms underlying such properties, and the physiological role of hemoglobin in respiratory gas transport.

Analysis of Oncogene Protein Structure Using Small World Network Concept

2020 ◽  
Vol 15 (7) ◽  
pp. 732-740
Author(s):  
Neetu Kumari ◽  
Anshul Verma
Keyword(s):  
Amino Acids ◽  
Protein Structure ◽  
Degree Distribution ◽  
Protein Structures ◽  
Small World ◽  
Extreme Condition ◽  
Centrality Measures ◽  
Small World Network ◽  
Network Concept ◽  
Oncogene Protein

Background: The basic building block of a body is protein which is a complex system whose structure plays a key role in activation, catalysis, messaging and disease states. Therefore, careful investigation of protein structure is necessary for the diagnosis of diseases and for the drug designing. Protein structures are described at their different levels of complexity: primary (chain), secondary (helical), tertiary (3D), and quaternary structure. Analyzing complex 3D structure of protein is a difficult task but it can be analyzed as a network of interconnection between its component, where amino acids are considered as nodes and interconnection between them are edges. Objective: Many literature works have proven that the small world network concept provides many new opportunities to investigate network of biological systems. The objective of this paper is analyzing the protein structure using small world concept. Methods: Protein is analyzed using small world network concept, specifically where extreme condition is having a degree distribution which follows power law. For the correct verification of the proposed approach, dataset of the Oncogene protein structure is analyzed using Python programming. Results: Protein structure is plotted as network of amino acids (Residue Interaction Graph (RIG)) using distance matrix of nodes with given threshold, then various centrality measures (i.e., degree distribution, Degree-Betweenness correlation, and Betweenness-Closeness correlation) are calculated for 1323 nodes and graphs are plotted. Conclusion: Ultimately, it is concluded that there exist hubs with higher centrality degree but less in number, and they are expected to be robust toward harmful effects of mutations with new functions.

A pair-to-pair amino acids substitution matrix and its applications for protein structure prediction

2007 ◽  
Vol 67 (1) ◽  
pp. 142-153 ◽  
Author(s):  
Eran Eyal ◽  
Milana Frenkel-Morgenstern ◽  
Vladimir Sobolev ◽  
Shmuel Pietrokovski
Keyword(s):  
Amino Acids ◽  
Protein Structure ◽  
Protein Structure Prediction ◽  
Structure Prediction ◽  
Substitution Matrix

Application of ionic liquids based on imidazole to the electrophoretic determination of amino acids in urine

2015 ◽  
Vol 70 (11) ◽  
pp. 1354-1359 ◽  
Author(s):  
E. A. Kolobova ◽  
L. A. Kartsova ◽  
E. A. Bessonova
Keyword(s):  
Amino Acids ◽  
Ionic Liquids
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