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Function and Flexibility: Friend or Foe?

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Book Series: Frontiers Research Topics ISSN: 16648714 ISBN: 9782889199723 Year: Pages: 102 DOI: 10.3389/978-2-88919-972-3 Language: English
Publisher: Frontiers Media SA
Subject: Science (General)
Added to DOAB on : 2016-01-19 14:05:46
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Abstract

Louis Sullivan (1856 - 1924) revolutionized architecture by designing the first skyscraper and he became famous by proclaiming that “form follows function”. When x-ray crystallographers visualized the structures of proteins for the first time, the structural biology field embraced the view that “function follows form” as the 3D-architecture of proteins could unveil various aspects of their function. Despite the original “1 gene - 1 protein structure - 1 function” relationship, nowadays a far more complicated picture emerges where the flexibility and dynamics of a protein can play a central role in a multitude of functions. The ultimate form(s) that a protein adopt when interacting with (a) partner molecule(s) are the most biologically relevant and in this context Sullivan’s quote is still appropriate: the conformation that the protein adopts follows from the function of that protein. Despite the fact that many well-characterized proteins have a well-folded structure, there is a growing interest in the conformational flexibility within proteins. This flexibility is also a balanced phenomenon: excess of flexibility can be detrimental for protein behaviour, as well as the lack thereof. Notwithstanding its importance, studying intrinsically disordered protein regions or conformational rearrangements can be a very challenging. Therefore, flexibility can be perceived as a friend or a foe, depending on the context. This e-book showcases the impact of the study of protein flexibility on the structural biology field and presents protein flexibility in the context of disease as well as its benign aspects. As detailed knowledge of the structural aspects of polypeptides remains essential to comprehend protein function, one of the future challenges for structural biology also lies with large macromolecular protein complexes. Also there the dynamics and flexibility are essential for proper functioning and molecular movement, which is an important aspect of living matter. This challenge stimulated the development of advanced techniques to study protein flexibility and the use of those techniques to address fundamental biological and biomedical problems. Those innovations should help us to unravel the intimate link between protein function and flexibility and explore new horizons.

In-Cell NMR Spectroscopy: Biomolecular Structure and Function

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ISBN: 9783039282548 / 9783039282555 Year: Pages: 152 DOI: 10.3390/books978-3-03928-255-5 Language: eng
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Science (General) --- Biology
Added to DOAB on : 2020-06-09 16:38:57
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This Special Issue examines state-of-the-art in-cell NMR spectroscopy as it relates to biological systems of increasing complexity. The compendia of research and recent innovations from prominent laboratories in the field of solid state and solution in-cell NMR spectroscopy, metabolomics and technology development are presented. The work establishes in-cell NMR spectroscopy as the premier method for determining the structures and interaction capabilities of biological molecules at high resolution within the delicately intricate interior of living cells, and the means of utilizing cells as living laboratories to directly assess the effects of exogenous and endogenous stimuli on cell physiology.]

Lipopolysaccharides (LPSs)

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ISBN: 9783039282562 9783039282579 Year: Pages: 390 DOI: 10.3390/books978-3-03928-257-9 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Medicine (General) --- Allergy and Immunology
Added to DOAB on : 2020-04-07 23:07:08
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The cytoplasm of Gram-negative bacteria is bound by three layers: an inner membrane, a layer of peptidoglycan, and an outer membrane. The outer membrane is an asymmetric lipidic bilayer, with phospholipids on its inner surface and lipopolysaccharides (LPSs) on the outside, with the latter being the major component of the outer leaflet and covering nearly three-quarters of the total outer cell surface. All LPSs possess the same general chemical architecture independently of bacterial activity (pathogenic, symbiotic, commensal), ecological niche (human, animal, soil, plant, water), or growth conditions. Endotoxins are large amphiphilic molecules consisting of a hydrophilic polysaccharide component and a covalently bound hydrophobic and highly conserved lipid component, termed lipid A (the endotoxin subunit). The polysaccharide component can be divided into two subdomains: the internal and conserved core region as well as the more external and highly variable O-specific chain, also referred to as the O-antigen due to its immunogenic properties. LPSs are endotoxins, one of the most potent class of activators of the mammalian immune system; they can be released from cell surfaces of bacteria during multiplication, lysis, and death. LPS can act through its biological center (lipid A component) on various cell types, of which macrophages and monocytes are the most important.

Keywords

aspirin --- hepcidin --- P65 (nuclear factor-?B) --- IL-6/JAK2/STAT3 pathway --- lipopolysaccharide (LPS) --- nitric oxide (NO) --- iron regulatory protein 1 (IRP1) --- Megalobrama amblycephala --- lipopolysaccharide induced TNF? factor --- lipopolysaccharide stimulation --- innate immune --- Aeromonas --- genomics --- inner core oligosaccharide --- outer core oligosaccharide --- lipopolysaccharide --- lipopolysaccharide --- Erwinia amylovora --- NMR --- ESI FT-ICR --- structural determination --- Bordetellae --- Bordetella holmesii --- endotoxin --- lipid A --- structure --- mass spectrometry --- genomic --- Edwardsiella tarda --- core oligosaccharide --- MALDI-TOF MS --- ESI MSn --- NMR --- genomic --- LPS tolerance --- hypothalamic inflammation --- insulin resistance --- pJNK --- fibroblast --- keratocyte --- cornea --- lipopolysaccharide --- bacteria --- chemokine --- adhesion molecule --- collagen --- tear fluid --- serum resistance --- complement --- Salmonella --- lipopolysaccharide --- sialic acid --- reptile-associated salmonellosis --- sepsis --- time response --- inflammation --- oxidative stress --- endotoxaemia --- mouse --- rat --- lipopolysaccharide --- double-stranded RNA --- epithelial cell --- dendritic cell --- allergic respiratory disorder --- hygiene hypothesis --- rhinovirus --- respiratory syncytial virus --- toll-like receptor --- LPS --- lipopolysaccharide --- heptosyltransferase --- protein dynamics --- glycosyltransferase --- GT-B --- inhibitor design --- lipopolysaccharide --- Coxiella burnetii --- Q fever --- phagosome --- virenose --- Plesiomonas shigelloides --- O-antigen --- lipopolysaccharide --- O-acetylation --- d-galactan I --- HR-MAS --- NMR spectroscopy --- endotoxin --- lipopolysaccharide --- Low Endotoxin Recovery --- phase transitions --- polysorbate --- LPS aggregates --- Small Angle X-ray Scattering --- MAT --- LAL and LER --- anti-conjugate serum --- core oligosaccharide --- lipopolysaccharide --- NMR spectroscopy --- ESI MS --- Proteus penneri

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