• polymers
  • Another fabrication method is ink-jetting, a drop-on-demand, non-contact method of dispersing the protein polymers onto the solid surface in the desired pattern. (wikipedia.org)
  • chemical
  • Virtually all the complex chemical functions of the living cell are performed by protein-based catalysts called enzymes. (wikibooks.org)
  • In addition to their catalytic functions, proteins can transmit and commute signals from the extracellular environment, duplicate genetic information, assist in transforming the energy in light and chemicals with astonishing efficiency, convert chemical energy into mechanical work, and carry molecules between cell compartments. (wikibooks.org)
  • A series of chemical treatments then enables deposition of the protein in the desired pattern upon the material underneath the photomask. (wikipedia.org)
  • Chemical modification of surfaces has been successfully applied in several instances to immobilize proteins in order to obtain valuable information. (wikipedia.org)
  • substrates
  • Terminal amine isotopic labeling of substrates (TAILS) is a method in quantitative proteomics that identifies the protein content of samples based on N-terminal fragments of each protein (N-terminal peptides) and detects differences in protein abundance among samples. (wikipedia.org)
  • The TAILS method has a number of applications including the identification of new substrates and proteases (including those that have an unknown and broad specificity) and as a way to define the termini of proteins that enables protein annotation. (wikipedia.org)
  • peptides
  • Like other methods based on N-terminal peptides, this assay uses trypsin to break proteins into fragments and separates the N-terminal peptides (the fragments containing the N-termini of the original proteins) from the other fragments (internal tryptic peptides). (wikipedia.org)
  • Alternative methods that rely on the free amino group of the N-terminus to identify the N-terminal peptides cannot detect some N-termini because they are "naturally blocked" (i.e. the natural protein does not have a free amino group). (wikipedia.org)
  • However, it identifies ~ 50% of proteins by two or more different and unique peptides (one of the original mature N-terminus and/or one or more neo-N-terminal peptide via cleavage site) that do not represent independent biological events thus cannot be averaged for quantification[clarification needed]. (wikipedia.org)
  • The labeled N-termini of the original proteins remain blocked, while the new internal tryptic peptides have a free N-terminus. (wikipedia.org)
  • Cytochrome
  • The denaturation of Thermus thermophilus cytochrome c-552 by acid, guanidine hydrochloride, and heat was studied by measuring the changes in absorption and circular dichroism. (biomedsearch.com)
  • amino acid
  • Arginine is a basic amino acid that is found in the active centers of proteins. (reference.com)
  • In the present study, an 11-amino acid domain of TAT protein which has been demonstrated to be able to transduce across cell membranes was fused with p53. (biomedsearch.com)
  • A protein is created by ribosomes that "read" RNA that is encoded by codons in the gene and assemble the requisite amino acid combination from the genetic instruction, in a process known as translation. (wikipedia.org)
  • structures
  • The folding of the protein, caused by structures and attractions between different parts of the protein, exposes or hides its different regions, determining how it reacts to its environment. (reference.com)
  • Structures of water-soluble proteins have a hydrophobic core in which side chains are buried from water, which stabilizes the folded state. (wikipedia.org)
  • side-chains
  • Minimizing the number of hydrophobic side chains exposed to water is the principal driving force behind the folding process, although formation of hydrogen bonds within the protein also stabilizes protein structure. (wikipedia.org)
  • chemically
  • It is theorized that prions may be able to act as a structural template for other chemically (but not structurally) identical proteins, but they can't function as a native template for protein synthesis de novo . (wikibooks.org)
  • One alternative involves the interaction of chemically modified surfaces with proteins under non-denaturing circumstances. (wikipedia.org)
  • Salts
  • We have previously found that the deactivating effects of salts on proteins can be correlated to an indicator of ion hydration, the B-viscosity coefficient of the anion in solution. (biomedsearch.com)
  • Cast formation is pronounced in environments favoring protein denaturation and precipitation (low flow, concentrated salts, low pH). (wikipedia.org)
  • urea
  • We also measure mRFP deactivation in solutions containing denaturants (guanidinium chloride or urea) or stabilizing co-solutes (glycerol or sucrose) frequently encountered in many protein formulations to test whether hydration of these co-solutes can be used to indicate their relative effects on protein kinetic stability. (biomedsearch.com)
  • Trimethylamine oxide also serves to counteract the protein-destabilizing tendencies of urea and pressure. (wikipedia.org)
  • analysis
  • HEX I dose not increase in leucocytes, tears and other body tissues but because of technical difficulties in these assays we examined the feasibility of using a radioimmunoassay for HEX A. By univariate analysis, the heat denaturation assay gave a lower cost of misclassification for non-pregnant normals while RIA did so for pregnant normals. (biomedsearch.com)
  • Bayesian analysis of bivariate gaussian density functions for heat denaturation and for radioimmunoassay of HEX isoenzymes was employed to calculate misclassification frequencies. (biomedsearch.com)
  • Other related techniques include dot blot analysis, quantitative dot blot, immunohistochemistry, and immunocytochemistry where antibodies are used to detect proteins in tissues and cells by immunostaining, and enzyme-linked immunosorbent assay (ELISA). (wikipedia.org)
  • Protein microarrays replace traditional proteomics techniques such as 2D gel electrophoresis or chromatography, which were time consuming, labor-intensive and ill-suited for the analysis of low abundant proteins. (wikipedia.org)
  • Nanoscale analysis of proteins using atomic force microscopy (AFM) requires surfaces with well-defined topologies and chemistries for many experimental techniques. (wikipedia.org)
  • hydration
  • Here, we test the influence of cations on protein kinetic stability by observing deactivation of mRFP (monomeric red fluorescent protein) in ammonium, caesium and chloride salt solutions, and we find that mRFP deactivation does not depend on cation hydration. (biomedsearch.com)
  • Tryptophan
  • The accessibility of the single tryptophan in Rev monomer to acrylamide quenching increases with decreasing protein concentration. (biomedsearch.com)
  • In the case of protein folding, the hydrophobic effect is important to understanding the structure of proteins that have hydrophobic amino acids (such as glycine, alanine, valine, leucine, isoleucine, phenylalanine, tryptophan and methionine) clustered together within the protein. (wikipedia.org)
  • biological
  • This is in contrast to intrinsically unstructured proteins, which are unfolded in their native state, but still functionally active and tend to fold upon binding to their biological target. (wikipedia.org)
  • functions
  • The chosen solid surface is then covered with a coating that must serve the simultaneous functions of immobilising the protein, preventing its denaturation, orienting it in the appropriate direction so that its binding sites are accessible, and providing a hydrophilic environment in which the binding reaction can occur. (wikipedia.org)
  • 1938
  • Greenstein (1938, 1939), however, appears to be the first to discover the high denaturing action of guanidinium halides and thiocyanates in following the liberation of sulfhydryl groups in ovalbumin and few other proteins as a function of salt concentration. (wikipedia.org)
  • structure
  • The written list of the amino acids linked together in a protein, in order, is called its primary structure. (wikibooks.org)
  • Thus, this study was initiated to monitor the structure of Rev as a function of protein concentration. (biomedsearch.com)
  • Once this post-translational modification process has been completed, the protein begins to fold (sometimes spontaneously and sometimes with enzymatic assistance), curling up on itself so that hydrophobic elements of the protein are buried deep inside the structure and hydrophilic elements end up on the outside. (wikipedia.org)
  • Its structure comes from whipped egg whites known as a protein foam. (wikipedia.org)
  • cell
  • What part of the cell makes proteins? (reference.com)
  • The transduction of His-TAT-p53 fusion protein into the human osteogenic sarcoma cell line (Saos-2) and its influence on cell cycle arrest and apoptosis. (biomedsearch.com)
  • If proteins in a living cell are denatured, this results in disruption of cell activity and possibly cell death. (wikipedia.org)
  • Some research has found that the copper significantly increases the dilatational elasticity, which is the elasticity of the protein cell wall at the interface of air/water. (wikipedia.org)
  • The quantity of mRNA in the cell often doesn't reflect the expression levels of the proteins they correspond to. (wikipedia.org)
  • Since it is usually the protein, rather than the mRNA, that has the functional role in cell response, a novel approach was needed. (wikipedia.org)
  • whites
  • A classic example of denaturing in proteins comes from egg whites, which are typically largely egg albumins in water. (wikipedia.org)
  • uniform
  • SDS is generally used as a buffer (as well as in the gel) in order to give all proteins present a uniform negative charge, since proteins can be positively, negatively, or neutrally charged. (wikipedia.org)
  • The proteins also adopt a more uniform orientation on the surface. (wikipedia.org)
  • molecular
  • According to the Central Dogma of Molecular Biology (proposed by Francis Crick in 1958), information is transferred from DNA to RNA to proteins. (wikibooks.org)
  • The western blot (sometimes called the protein immunoblot) is a widely used analytical technique used in molecular biology, immunogenetics and other molecular biology disciplines to detect specific proteins in a sample of tissue homogenate or extract. (wikipedia.org)
  • high
  • They are pathognomonic for high urinary protein nephrotic syndrome. (wikipedia.org)
  • The high-throughput technology behind the protein microarray was relatively easy to develop since it is based on the technology developed for DNA microarrays, which have become the most widely used microarrays. (wikipedia.org)