09_chapter 4
... that of the functional group attached to the resin in order to bind. For example, immunoglobulins, which generally have an overall positive charge, will bind well to cation exchangers, which contain negatively charged functional groups. Because this interaction is ionic, binding must take place unde ...
... that of the functional group attached to the resin in order to bind. For example, immunoglobulins, which generally have an overall positive charge, will bind well to cation exchangers, which contain negatively charged functional groups. Because this interaction is ionic, binding must take place unde ...
Coupling Coherence Distinguishes Structure Sensitivity in Protein
... Our heme-protein analysis indicates that exponential distance dependence for protein ET rates occurs in the small C multiple-pathway regime. Because small C values have been computed in nonheme proteins as well, we can further explore the correlation between small C values and exponential distance d ...
... Our heme-protein analysis indicates that exponential distance dependence for protein ET rates occurs in the small C multiple-pathway regime. Because small C values have been computed in nonheme proteins as well, we can further explore the correlation between small C values and exponential distance d ...
Cooperative Function of Upstream and Core Domains of the Yeast
... We have previously reported that the yeast, Saccharomyces cerevisiae, ribosomal gene promoter contains at least two essential domains, an upstream domain located at the 5' boundary near position - 150 and a core domain around the site of transcription initiation at + 1, by in vitro analysis using wh ...
... We have previously reported that the yeast, Saccharomyces cerevisiae, ribosomal gene promoter contains at least two essential domains, an upstream domain located at the 5' boundary near position - 150 and a core domain around the site of transcription initiation at + 1, by in vitro analysis using wh ...
Structural Influences: Cholesterol, Drug, and Proton Binding to Full
... mixture: Ala-Ile, Ile-Leu, Val-Leu, and Phe-Leu. The first three samples were prepared to search for unambiguous interhelical distance restraints between amino acids of different types in the TM helices and the last sample was prepared for a similar search between the amphipathic helices and the adj ...
... mixture: Ala-Ile, Ile-Leu, Val-Leu, and Phe-Leu. The first three samples were prepared to search for unambiguous interhelical distance restraints between amino acids of different types in the TM helices and the last sample was prepared for a similar search between the amphipathic helices and the adj ...
PERG Survey (2007) Bottlenecks in Protein Expression The goal of
... What is the most frequent problem encountered with insect cell expression systems? Low expression / Secretion into media ...
... What is the most frequent problem encountered with insect cell expression systems? Low expression / Secretion into media ...
Computational Tools For Protein Modeling
... well for global alignment. BLAST is the most widely used local alignment tool. It is also the fastest tool generally available (a pairwise alignment typically can be finished in seconds). Another reason for being widely used is that BLAST gives an expectation value for an alignment, which estimates ...
... well for global alignment. BLAST is the most widely used local alignment tool. It is also the fastest tool generally available (a pairwise alignment typically can be finished in seconds). Another reason for being widely used is that BLAST gives an expectation value for an alignment, which estimates ...
the scf ubiquitin ligase: insights into a molecular machine
... (LRR)), the domain is an arc-shaped α–β-repeat structure that is also found in many protein-binding contexts, including the extracellular-binding domain of certain surface receptors11,12. In most cases, FBLs also seem to involve substrate phosphorylation for their interaction, but this does not seem ...
... (LRR)), the domain is an arc-shaped α–β-repeat structure that is also found in many protein-binding contexts, including the extracellular-binding domain of certain surface receptors11,12. In most cases, FBLs also seem to involve substrate phosphorylation for their interaction, but this does not seem ...
prosite.excerpt
... Class IIa bacteriocins contain between 37 and 48 residues. Based on their primary structures, the peptide chains of class IIa bacteriocins may be divided roughly into two regions: a hydrophilic, cationic and highly conserved N-terminal region, and a less conserved hydrophobic/amphiphilic Cterminal r ...
... Class IIa bacteriocins contain between 37 and 48 residues. Based on their primary structures, the peptide chains of class IIa bacteriocins may be divided roughly into two regions: a hydrophilic, cationic and highly conserved N-terminal region, and a less conserved hydrophobic/amphiphilic Cterminal r ...
Releasable conjugation of polymers to proteins
... permit the selective modification of all solvent exposed amino acid residues of a given sort. There currently exist residue-specific reactions for permanently coupling polymers to at least 10 out of the 20 canonical amino acids found in proteins.7-10 However, in many cases, polymer-modification can ...
... permit the selective modification of all solvent exposed amino acid residues of a given sort. There currently exist residue-specific reactions for permanently coupling polymers to at least 10 out of the 20 canonical amino acids found in proteins.7-10 However, in many cases, polymer-modification can ...
Disruption of CEP290 microtubule/membrane-binding domains
... Projecting CEP290 aa 1–362 onto an α-helical wheel, a segment from aa 257 to 292 was predicted to form a canonical amphipathic α-helix (Figure 3B). Such helices have been shown to be critical in mediating robust interactions between peripheral membrane proteins and various cellular membranes (35). C ...
... Projecting CEP290 aa 1–362 onto an α-helical wheel, a segment from aa 257 to 292 was predicted to form a canonical amphipathic α-helix (Figure 3B). Such helices have been shown to be critical in mediating robust interactions between peripheral membrane proteins and various cellular membranes (35). C ...
Notes for using PROTPOL.f
... NARO = no. of aromatic (PHE+TYP+TRP) side chains NSUB = no. of subunits (distinct from number of chains – all subunits must be equivalent. i. e., have the same number of peptides, aromatics, disulfides, Pro. A given subunit can consist of more than one chain and chains can and do generally differ in ...
... NARO = no. of aromatic (PHE+TYP+TRP) side chains NSUB = no. of subunits (distinct from number of chains – all subunits must be equivalent. i. e., have the same number of peptides, aromatics, disulfides, Pro. A given subunit can consist of more than one chain and chains can and do generally differ in ...
Gene Section STK4 (serine/threonine kinase 4) Atlas of Genetics and Cytogenetics
... STK4 plays a role in promoting apotosis, in particular, in chromosome condensation during programmed cell death. STK4 is cleaved by caspase 3 during apoptosis, releasing the highly active N-terminal kinase domain. This active protein promotes apoptosis by activating JNK and also by further caspase a ...
... STK4 plays a role in promoting apotosis, in particular, in chromosome condensation during programmed cell death. STK4 is cleaved by caspase 3 during apoptosis, releasing the highly active N-terminal kinase domain. This active protein promotes apoptosis by activating JNK and also by further caspase a ...
Phosphoproteomics reveals extensive in vivo phosphorylation of
... and turnover of the protein involved. In the past, however, the analysis of phosphorylation sites of proteins has been a great challenge. In the last few years there has been an explosive growth in the amount of studies describing the use of immobilized metal affinity chromatography (IMAC) (1) or ot ...
... and turnover of the protein involved. In the past, however, the analysis of phosphorylation sites of proteins has been a great challenge. In the last few years there has been an explosive growth in the amount of studies describing the use of immobilized metal affinity chromatography (IMAC) (1) or ot ...
Protein domain
A protein domain is a conserved part of a given protein sequence and (tertiary) structure that can evolve, function, and exist independently of the rest of the protein chain. Each domain forms a compact three-dimensional structure and often can be independently stable and folded. Many proteins consist of several structural domains. One domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. Domains vary in length from between about 25 amino acids up to 500 amino acids in length. The shortest domains such as zinc fingers are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be ""swapped"" by genetic engineering between one protein and another to make chimeric proteins.