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Macronutrients
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
Globular or corpuscular proteins possess a relatively spherical or ovoid shape and are usually water-soluble (36, 47). Globular proteins are generally more sensitive to temperature and pH change than their fibrous counterparts. Typically, globular proteins play an essential role in metabolism and have several other dynamic functions. Globular proteins include enzymes, cytochrome C, nutrient proteins, reserve proteins, myosin in muscle, and blood proteins such as serum albumin, glycoproteins, hemoglobin, immunoglobulins (antibodies), and hormones (36, 47). Hemoglobin is used to transport oxygen, and albumin is a carrier of fatty acids in blood.
Proteins for Conditioning Hair and Skin
Published in Randy Schueller, Perry Romanowski, Conditioning Agents for Hair and Skin, 2020
Globular proteins (protein chains compactly folded) include many which are water soluble, such as serum albumin, hemoglobin, and catalase. As a general rule, these proteins are more susceptible to denaturation (permanent loss of native conformation and hence biochemical function) at high temperature, low concentration, extremes of pH, and air/solution interfaces (i.e., in foams) than are fibrous proteins (2).
Inherited Disorders of Red Cell Membrane Proteins
Published in Ronald L. Nagel, Genetically Abnormal Red Cells, 2019
Ankyrin is a 210,000-dalton protein which runs as band 2.1 in the SDS-PAGE system illustrated in Figure 1. Although there are no documented inherited defects of this protein to date, it is described here because of its critical position as a bridging protein, attaching spectrin to protein 3. Two structural and functional domains of this globular protein have been identified.38,39 As seen in Figure 2, ankyrin is a bipolar molecule whose neutral phos-phorylated region binds to the ankyrin-binding site of the β chain of spectrin, and a relatively basic region which binds to the negatively charged cytoplasmic portion of protein 3.
Protease resistance of ex vivo amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies
Published in Amyloid, 2021
Jonathan Schönfelder, Peter Benedikt Pfeiffer, Tejaswini Pradhan, Johan Bijzet, Bouke P. C. Hazenberg, Stefan O. Schönland, Ute Hegenbart, Bernd Reif, Christian Haupt, Marcus Fändrich
A potential third factor that may be added based on the present findings is the need to form a highly stable fibril state. In the case of native folding reactions that lead to globular proteins it is known that only a limited number of polypeptide chains possesses an appropriate amino acid sequence to form these compact protein states. As a result, there are many so-called intrinsically disordered proteins that are unable to fold into compact globular conformations [52]. In case of amyloid fibrils, we suggest that although the formation of such fibrils is a common property of polypeptide chains with an appropriate backbone structure there will be differences in the stability of fibrils in particular to proteolytic digestion. These differences may arise from the specific packing of fibril protein segments that depend on the amino acid sequence and on the presence of a specific, and complementary, arrangement of side chains. As a result, the number of amino acid sequences that allow the formation of pathogenic amyloid fibrils will be smaller than the number of proteins that can form any type of cross-β fibril.
Taenia solium proteins: a beautiful kaleidoscope of pro and anti-inflammatory antigens
Published in Expert Review of Proteomics, 2020
The evolution of high throughput techniques are boon to biologists, specially to study complex extracellular parasites, which undergoes metamorphosis from egg to adult in several stages and in different hosts. The major limitations in studying cestodes have been the unavailability of good quality, reliable genomic and proteomic database. Tsai et. al., (2013) sequenced four adult tapeworms and revealed the host-dependent survival nature of these cestode parasites. Though the electronic annotation specifically to T. solium is still not available, but by using sequence alignment tools we attempted to gain knowledge about this parasite’s protein profile. It is a host-dependent parasite that’s why it lacks all-inclusive machinery for synthesis of biomolecules essential for survival and has a very complex proteome make-up with diverse functions [17,39]. The parasite protein’s VF and ESPs behave differently inside the host and carry out different functions which were substantiated from their shared, yet unique protein abundance pattern noticed in this study. The VF was having more globular protein (GRAVY below 0) than membrane-bound proteins. Globular proteins are water soluble in nature and are transported easily as compared to membrane-bound, which require complex machinery and have been found to be involved in binding, catalysis, transport, immunity, cellular metabolism, and many more. Thus, underlying the importance of VF proteins for survival of parasite.
Computational re-design of protein structures to improve solubility
Published in Expert Opinion on Drug Discovery, 2019
Susanna Navarro, Salvador Ventura
These sequence-based aggregation predictors perform accurately for proteins displaying extended or partially unfolded conformations, because their APRs are exposed to solvent. They have become powerful tools to study the aggregation determinants of pathogenic intrinsically disordered proteins such as Aβ42, α-synuclein, tau or amylin, allowing to evaluate the impact of genetic mutations on their aggregation rates. However, a new conceptual scenario is needed when dealing with globular proteins. The majority of these proteins bury sequential APRs into their hydrophobic core or engage them in the cooperative non-covalent interactions that sustain their secondary and tertiary structures, excluding them from undesired intermolecular contacts [61]. Thus, their APRs are irrelevant for the aggregation of natively folded states. In addition, in many cases, APRs can be exposed at the surface of globular proteins playing a functional role in protein-protein binding [62,63]. These APRs are often formed by non-consecutive residues arranged in structural proximity, not being effectively identified by the sequence-based algorithms.