Sentences with phrase «peptide bonded»

When you combine the powerful, muscle building effects of Leucine (in peptide bonded form for even greater absorption) with a precision blend of the 3 best sources of whey protein available (Whey Isolate, Whey Concentrate and Hydrolysed whey Isolate), then you have a serious muscle - building Whey protein product.

PhD are the only brand in sports nutrition to add peptide bonded Leucine peptides to our Whey protein product, which sets the formula apart from the usual, generic online brands supplying whey as a commodity.

Here's what's going on when protein is cooked: As a protein is heated, its surface area shrinks, making it harder for digestive enzymes to get in there and start breaking down those peptide bonds.

The team's first version of a flow - based peptide synthesis machine, reported in 2014, sped up the process to about three minutes per peptide bond.

EF - P facilitates the proper positioning of the fMet - tRNAifMet for the formation of the first peptide bond during translation initiation.

Elongation factor P (EF - P) is an essential protein that stimulates the formation of the first peptide bond in protein synthesis.

Biochemical and crystallographic evidence suggests that 23S ribosomal RNA (rRNA) is the catalyst of peptide bond formation.

Both substrate analogs are contacted exclusively by conserved ribosomal RNA (rRNA) residues from domain V of 23S rRNA; there are no protein side - chain atoms closer than about 18 angstroms to the peptide bond being synthesized.

These results are consistent with a mechanism wherein the nucleotide base of A2451 serves as a general acid base during peptide bond formation.

One of the molecules, acetamide, is particularly exciting because it contains a peptide bond, the essential bond for connections between amino acids.

These two molecules promote the formation of peptide bonds that link amino acids into a new protein, the team reports in tomorrow's issue of Science (see Ban et al. and Nissen et al.).

«Every peptide bond requires consuming energy, and the movement of the mRNA relative to the ribosome requires energy,» he says.

A peptide bond is a chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, releasing a molecule of water (H2O).

The molecule, methyl isocyanate, has a structure that is chemically similar to a peptide bond, which is what holds amino acids together in proteins.

Since proteins are an important part of the diet, the stomach and intestines harbor countless enzymes that break peptide bonds.

This study not only establishes that the substitutions of the peptide bonds in FC131 (except for the D - Tyr - Arg position) with an amidine motif improves the CXCR4 inhibitory activity, but also demonstrates that these analogues are selective antagonists for CXCR4 without affecting CXCR7 or CCR5 activity.

The cis / trans isomerization of peptide bonds represents one of the most fundamental chemical processes governing the biochemical properties of proteins.

In a separate study, the substitution of peptide bond carbonyl (CO) groups with imino (C = NH) groups has been taken into consideration and a series of amidine - containing FC131 analogues (9 - 15), in which each peptide bond was replaced with the amidine substructure, have been designed (Table 1)[70, 77].

Peptide bond mimicry by (E)- alkene and (Z)- fluoroalkene peptide isosteres: synthesis and bioevaluation of alpha - helical anti-HIV peptide analogues.

It is now well known that a systematic replacement of the planar peptide bond with an alkene bioisostere is useful for the estimation of the electrostatic effects and for the SAR evaluation of peptide derivatives.

On the basis of these considerations, the effects of the Arg2 - Arg3 and Arg3 - Nal4 peptide bonds on the activity of FC131 have been investigated through the synthesis and evaluation of the alkene analogues such as compounds 5 - 8 (Figure 6)[69].

The replacement of the Arg3 - Nal4 peptide bond with an (E)- alkene isostere in compound 7 produced a negative effect on CXCR4 inhibitory activity, probably due to the lack of H - bonding of amide moiety and a different interaction of pseudo -1,3-allylic strain between the Arg3 carbonyl group and the Nal4 side chain.

Our laboratory experiments show that methyl isocyanate can indeed be produced on icy particles under very cold conditions that are similar to those in interstellar space This implies that this molecule — and thus the basis for peptide bonds — is indeed likely to be present near most new young solar - type stars,» said Niels Ligterink at the Leiden Observatory in the Netherlands.

Peptide bond - hydrolyzing catalytic antibodies (catabodies) could degrade toxic proteins, but acquired immunity principles have not provided evidence for beneficial catabodies.

«This implies that this molecule, and thus the basis for peptide bonds, is indeed likely to be present near most new young solar - type stars,» writes Niels Ligterink, from Sackler Laboratory for Astrophysics at Leiden Observatory, the Netherlands.

Having the mRNA as a blueprint, the ribosome begins to take the amino acids within the intracellular pool and start connecting them together with peptide bonds to form new contractile proteins.

Essentially, this acts as a method of «pre-digesting» the protein by separating (i.e. lysing) peptide bonds; hence the time for digestion and absorption of amino acids will be reduced.

Allergenza is a powerful formula uniquely designed with proprietary blends of enzymes, prebiotics and probiotics to break down gluten proteins by targeting both internal and external peptide bonds.

Dietary protein digestion normally begins in the stomach where pepsin, an acid - stable protease, initiates the cleavage of peptide bonds within proteins to produce large polypeptide molecules.

Complete digestion of these polypeptides should occur in the duodenum and jejunum where pancreatic and intestinal proteases and peptidases cleave peptide bonds until only small peptide units and individual amino acids remain.

Alkaline protease is a group of microbial - derived enzymes that have their optimal proteolytic activity at an alkaline pH. Aklaline protease also breaks down a variety of peptide bonds both within and from the ends of a protein chain.

Acid protease is a group of microbial - derived enzymes that have their optimal proteolytic activity at an acidic pH. Acid protease hydrolyzes a broad array of peptide bonds and exhibits both endo - and exoprotease activities meaning it breaks peptide bonds within and from the ends of a protein chain and giving rise to amino acids and small polypeptides.

Glutenza ™ is a gluten pulverizing formula uniquely designed with powerful enzymes, prebiotics and probiotics to break down gluten proteins by targeting both internal and external peptide bonds.

When we eat protein the body must break these peptide bonds in the digestive tract using proteases (for more information on proteases, please click here).

These subunits are linked together by peptide bonds to form chains that can be straight lines, or branched like the sub-branches on a tree.

Glutathione, you see, is called a tripeptide because he's composed of three amino acids, each bound together by a peptide bond that magnesium and ATP have infused with energy.

Protease are enzymes that break the peptide bonds that link amino acids into polypeptide chains forming proteins.

These beads are connected together by peptide bonds.

It breaks down proteins to form peptides and amino acids with preferential cleavage of peptide bonds, where the carbonyl group is from either a basic amino acid or an aromatic amino acid.

All plant and animal cells produce enzymes, made from protein molecules (long chains of amino acids held together by peptide bonds).

When proline is bound as an amide in a peptide bond, its nitrogen is not bound to any hydrogen, meaning it can not act as a hydrogen bond donor, but can be a hydrogen bond acceptor.

It also affects the rate of peptide bond formation between proline and other amino acids.

• Amino Acids • Peptide Bonds • Polypeptides and Proteins • Protein Structure • Protein Properties • Protein Classification • Importance of Protein in Food • Sources of Protein • Testing Foods: Biuret Test • Positive and Negative Results • What can go Wrong • Regulating Foods • Allergy Information

Not exact matches

The collagen has undergone a process of hydrolysis (separating the molecular bonds between collagen strands with an acid, like lime or enzymes) to reduce the protein into smaller peptides, which renders it more readily bioavailable.

Another major advantage the catalysts have is that, while they are general in what substrate they can oxidize, they are very specific about which carbon - hydrogen bonds they cut — so much so that they target a certain spot on amino acids like proline, leucine or valine even when they are part of a much larger peptide chain.

To remedy this, Bode discovered a new chemical reaction that creates amide bonds (a reaction between alpha - keto acid and hydroxylamine), which he uses to connect small, easily synthesized peptides — strands of amino acids — into longer peptides.

Miller's lab has been able to tune the bond - forming functions in peptide - based catalysts, which are similar to nature's enzymes in that they are composed of amino acids, but are orders of magnitude simpler in terms of their molecular size.

In another study in Science, Yale biochemist Scott Strobel describes an experiment that pinpoints one nucleotide base in the RNA as key for the peptide - bond reaction.

About ten negatively charged peptide combinations were identified that both adhere to and bond materials well.

The amino acid proline is special among the natural amino acids because it can not form hydrogen bonds to other structural parts of the peptide when integrated in a peptide.