Chapter 5 The Structure and Function of Large Biological Molecules
... 56) The R group or side chain of the amino acid serine is —CH 2 OH. The R group or side chain of the amino acid alanine is —CH 3 . Where would you expect to find these amino acids in a globular protein in aqueous solution? A) Serine would be in the interior, and alanine would be on the exterior of ...
... 56) The R group or side chain of the amino acid serine is —CH 2 OH. The R group or side chain of the amino acid alanine is —CH 3 . Where would you expect to find these amino acids in a globular protein in aqueous solution? A) Serine would be in the interior, and alanine would be on the exterior of ...
12. Molecular Recognition: The Thermodynamics of
... From The Molecules of Life by Kuriyan, Konforti & Wemmer © Garland Publishing, 2009. Distribution Prohibited. ...
... From The Molecules of Life by Kuriyan, Konforti & Wemmer © Garland Publishing, 2009. Distribution Prohibited. ...
Proteolytic processing in the secretory pathway of Aspergillus niger
... proteases. A brief explanation of these four groups is given here; a more elaborate description is given by van den Hombergh (1996). Each group has a different proteolytic mechanism and therefore different enzymatic characteristics and inhibitors. The cysteine proteases are a rare group of proteases ...
... proteases. A brief explanation of these four groups is given here; a more elaborate description is given by van den Hombergh (1996). Each group has a different proteolytic mechanism and therefore different enzymatic characteristics and inhibitors. The cysteine proteases are a rare group of proteases ...
Short peptides conferring resistance to macrolide antibiotics
... two distinct segments of the 23S rRNA located in close vicinity in the ribosome tertiary structure. The best characterized rRNA site involved in macrolide binding is a segment of the so called central loop of domain V, in which positions 2058 and 2059 (E. coli numbering) are critical for the drug bi ...
... two distinct segments of the 23S rRNA located in close vicinity in the ribosome tertiary structure. The best characterized rRNA site involved in macrolide binding is a segment of the so called central loop of domain V, in which positions 2058 and 2059 (E. coli numbering) are critical for the drug bi ...
Structure based hypothesis of a mitochondrial
... Termination of protein synthesis in the ribosome is signaled by nonsense codons, known as ochre (UAA), opal (UGA) and amber (UAG) [1,2]. In contrast to the recognition of sense codons, no tRNA is involved in nonsense codon recognition. This role is taken over by class I release factor proteins. Like ...
... Termination of protein synthesis in the ribosome is signaled by nonsense codons, known as ochre (UAA), opal (UGA) and amber (UAG) [1,2]. In contrast to the recognition of sense codons, no tRNA is involved in nonsense codon recognition. This role is taken over by class I release factor proteins. Like ...
Structural Mechanisms for Regulation of Membrane
... suggested to be located under the Rab-binding platform in domain I based on the complex of RabGDI with a di-geranyl geranyl peptide (49). Curiously, however, subsequent structures of RabGDI and REP in complex with mono-geranyl geranyl Ypt1p and Rab7 revealed a distinct prenyl group pocket in domain ...
... suggested to be located under the Rab-binding platform in domain I based on the complex of RabGDI with a di-geranyl geranyl peptide (49). Curiously, however, subsequent structures of RabGDI and REP in complex with mono-geranyl geranyl Ypt1p and Rab7 revealed a distinct prenyl group pocket in domain ...
Manipulation of Epitope Function by Modification of Peptide
... infectious agents in humans. Glycoprotein D represents a major immunogenic component of the virion envelope. Using prediction analysis of the sequence of gD from HSV-1 and synthetic peptide-conjugates with branched polypeptide poly[Lys(DL-Alam)], (AK) where m3) the 281DPVG284 tetramer sequence has ...
... infectious agents in humans. Glycoprotein D represents a major immunogenic component of the virion envelope. Using prediction analysis of the sequence of gD from HSV-1 and synthetic peptide-conjugates with branched polypeptide poly[Lys(DL-Alam)], (AK) where m3) the 281DPVG284 tetramer sequence has ...
A C-terminus Mitochondrial-localization Region and BH3 Domain of
... 1972; Oppenheim 1991; Yoshida et al. 1998). One of the reasons that apoptosis is utilized for these functions is that unlike other modes of cell death, such as necrosis, apoptosis eliminates cells without eliciting an inflammatory response or causing damage to the surrounding tissue (Kerr et al. 197 ...
... 1972; Oppenheim 1991; Yoshida et al. 1998). One of the reasons that apoptosis is utilized for these functions is that unlike other modes of cell death, such as necrosis, apoptosis eliminates cells without eliciting an inflammatory response or causing damage to the surrounding tissue (Kerr et al. 197 ...
Bitis gabonica rhinoceros
... Competing Interests: The authors have declared that no competing interests exist. * E-mail: [email protected] ...
... Competing Interests: The authors have declared that no competing interests exist. * E-mail: [email protected] ...
ICoMST-Abstract_YUFU
... The homology assessment data from the BLAST analysis of two collagen sequences are displayed in Table 1; the “identities” serves as the proportion of matched amino acids in the entire length of the aligned sequences; i.e. the larger the identities, the more homology; the “positives” stands for the v ...
... The homology assessment data from the BLAST analysis of two collagen sequences are displayed in Table 1; the “identities” serves as the proportion of matched amino acids in the entire length of the aligned sequences; i.e. the larger the identities, the more homology; the “positives” stands for the v ...
THE DYNAMIN SUPERFAMILY: UNIVERSAL MEMBRANE
... nerve terminals114. This might be because uncoating of endocytic profiles occurs independently of scission. Indeed, the uptake of transferrin in COS cells is clathrindependent and mutants of dynamin that slow the scission reaction give rise to trapped vesicles that no longer have a clathrin coat87. ...
... nerve terminals114. This might be because uncoating of endocytic profiles occurs independently of scission. Indeed, the uptake of transferrin in COS cells is clathrindependent and mutants of dynamin that slow the scission reaction give rise to trapped vesicles that no longer have a clathrin coat87. ...
Amino acid frequency distribution at the enzymatic active site
... biochemical information, the three dimension structure of enzymes in complex with substrate has been used extensively to determine their catalytic mechanism. In general, the amino acids at the enzyme active site act as acid-base, nucleophiles or electrophiles and also make hydrogen bond either with ...
... biochemical information, the three dimension structure of enzymes in complex with substrate has been used extensively to determine their catalytic mechanism. In general, the amino acids at the enzyme active site act as acid-base, nucleophiles or electrophiles and also make hydrogen bond either with ...
Transporters of nucleotide sugars, nucleotide
... One would expect mammalian homozygotes in some Golgi transporter mutations to be lethal, as many transporters are highly specific and gene disruptions of glycosyltransferases acting downstream from these transporters were found to be so, that is, N-acetylglucosaminyltransferase I (Ioffe and Stanley, ...
... One would expect mammalian homozygotes in some Golgi transporter mutations to be lethal, as many transporters are highly specific and gene disruptions of glycosyltransferases acting downstream from these transporters were found to be so, that is, N-acetylglucosaminyltransferase I (Ioffe and Stanley, ...
Characterization and the role of carbonic anhydrase
... simultaneous requirement that minimal carbonic anhydrase activity be found within the cystol. The CAs are ubiquitous metallo enzymes (mainly Zn) that catalyzes the quick reversible hydration reaction of CO2 to HCO3and protons (H+) or vice versa. This “reverse” reaction gives CA its name, because it ...
... simultaneous requirement that minimal carbonic anhydrase activity be found within the cystol. The CAs are ubiquitous metallo enzymes (mainly Zn) that catalyzes the quick reversible hydration reaction of CO2 to HCO3and protons (H+) or vice versa. This “reverse” reaction gives CA its name, because it ...
fulltext - DiVA Portal
... Signal conduction as well as substance exchange through membranes, involving active and passive transport of ions, macromolecules and metabolites, are predominantly mediated by proteins. They are either an integral part of the membrane bilayer or are peripherally associated with it. Proteins involve ...
... Signal conduction as well as substance exchange through membranes, involving active and passive transport of ions, macromolecules and metabolites, are predominantly mediated by proteins. They are either an integral part of the membrane bilayer or are peripherally associated with it. Proteins involve ...
Recoding the Genetic Code with Selenocysteine
... proteome contains many essential modified proteins that culture) leads to fourfold higher yield of pure selenoprotein arise by posttranslational modification (PTM), and mismodicompared to the UGA-encoded selenoenzyme (0.9 mg L 1 fied proteins may lead to defects in cellular signaling and culture). T ...
... proteome contains many essential modified proteins that culture) leads to fourfold higher yield of pure selenoprotein arise by posttranslational modification (PTM), and mismodicompared to the UGA-encoded selenoenzyme (0.9 mg L 1 fied proteins may lead to defects in cellular signaling and culture). T ...
Protein relative abundance patterns associated with sucrose
... to catalog the functional potential of all microbial genes within a smaller subset of subjects. One of the key findings was that healthy sites from different people were broadly similar with respect to their functional profiles, even though there was extensive individual variation in their taxonomic ...
... to catalog the functional potential of all microbial genes within a smaller subset of subjects. One of the key findings was that healthy sites from different people were broadly similar with respect to their functional profiles, even though there was extensive individual variation in their taxonomic ...
Supplementary Online Materials
... and/or its repartitioning out of membranes. According to current membrane-topological folding theory[1,3-5], it is plausible that the acidichydrophobic amphipathic DIDLID/DLG element, Neh5L and AD2 regions would exist in a non-structural loop when they are unfolded in solution. However, differential ...
... and/or its repartitioning out of membranes. According to current membrane-topological folding theory[1,3-5], it is plausible that the acidichydrophobic amphipathic DIDLID/DLG element, Neh5L and AD2 regions would exist in a non-structural loop when they are unfolded in solution. However, differential ...
World Index of BioMolecular Visualization Resources
... lysozyme bound to antibody; disulfide bonds in immunoglobulin; complementaritydetermining regions in antibody; glycosylation of antibody, N-linked; lesson plan, antibody. At MolviZ.Org: A tutorial on IgG structure in Chime including an introduction to stick, ball and stick, spacefill renderings, pep ...
... lysozyme bound to antibody; disulfide bonds in immunoglobulin; complementaritydetermining regions in antibody; glycosylation of antibody, N-linked; lesson plan, antibody. At MolviZ.Org: A tutorial on IgG structure in Chime including an introduction to stick, ball and stick, spacefill renderings, pep ...
Comparative Analysis of Prothrombin Activators
... dependent, c-carboxyglutamic acid residue–rich region at the N-terminus of the light chain plays a critical role in the binding of phospholipids and calcium ions, while the heavy chain contains the catalytic site residues (Jackson 1984; Persson, Hogg, and Stenflo 1993). Prothrombin activators from s ...
... dependent, c-carboxyglutamic acid residue–rich region at the N-terminus of the light chain plays a critical role in the binding of phospholipids and calcium ions, while the heavy chain contains the catalytic site residues (Jackson 1984; Persson, Hogg, and Stenflo 1993). Prothrombin activators from s ...
The nonenzymatic subunit of pseutarin C, a
... physiologically relevant rate, FXa must form the “prothrombinase complex” with the nonenzymatic cofactor factor Va (FVa), calcium ions, and phospholipid membranes.1 Phospholipids stimulate prothrombin activation by lowering the Km for prothrombin2-4 and provide a surface on which FXa, FVa, and proth ...
... physiologically relevant rate, FXa must form the “prothrombinase complex” with the nonenzymatic cofactor factor Va (FVa), calcium ions, and phospholipid membranes.1 Phospholipids stimulate prothrombin activation by lowering the Km for prothrombin2-4 and provide a surface on which FXa, FVa, and proth ...
Chloroplast transit peptides: structure, function and evolution
... universal feature, the position and degree of amphipathicity of these two helices could vary. For instance, in trFd, NMR indicates that the N-terminal helix is amphipathic, whereas, in SStp, the C-terminal region is predicted to be amphipathic (Fig. 3). Such membrane-induced secondary structures in ...
... universal feature, the position and degree of amphipathicity of these two helices could vary. For instance, in trFd, NMR indicates that the N-terminal helix is amphipathic, whereas, in SStp, the C-terminal region is predicted to be amphipathic (Fig. 3). Such membrane-induced secondary structures in ...
Accumulation of xylem transported protein at pit membranes and
... pathway of least resistance during sap transport from one vessel to another. Nevertheless, they may account for around 50% of overall xylem resistance to flow (see review by Choat et al., 2008). Proteomic investigations using gel separations and, more recently, tandem mass spectrometry have identifi ...
... pathway of least resistance during sap transport from one vessel to another. Nevertheless, they may account for around 50% of overall xylem resistance to flow (see review by Choat et al., 2008). Proteomic investigations using gel separations and, more recently, tandem mass spectrometry have identifi ...
Protein
Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɨnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within living organisms, including catalyzing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than about 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.Once formed, proteins only exist for a certain period of time and are then degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal and or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyze biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. Proteins are also necessary in animals' diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food. Through the process of digestion, animals break down ingested protein into free amino acids that are then used in metabolism.Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.