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Tryptophan is a derivative of alanine and contains alkyl side chains. Tryptophan belongs to the aromatic group and is non-polar and hydophobic. Tryptophan has a functioning indole group which can hydrogen bond donate and is often in contact with the solvent (water) in folded proteins.
Alanine is non-polar as well and can also hydrogen bond and is called an aliphatic R group amino acid and is hydrophobic.
The biologically important amino acids have the amino group attached to the carbon atom next door to the -COOH group.
Amino acids have the general structural molecular formula -NH2CHRCOOH. They have two important functional groups (a functional group means a group of atoms in a molecule that have characteristic chemical reactions regardless of the rest of the molecule): carboxylic acid group -COOH and an amine group -NH2.
Two amino acids can undergo a condensation reaction to form a dipeptide. Further condensation reactions result in a polypeptide. The amino acid units are linked by peptide bonds (sometimes called peptide links).
R1-COOH + R2-NH2 --> R1-CO-NH-R2 + H2O R=a side group.
Tryptophan is a derivative of alanine and contains alkyl side chains. Tryptophan belongs to the aromatic group and is non-polar and hydophobic. Tryptophan has a functioning indole group which can hydrogen bond donate and is often in contact with the solvent (water) in folded proteins.
Alanine is non-polar as well and can also hydrogen bond and is called an aliphatic R group amino acid and is hydrophobic.
The biologically important amino acids have the amino group attached to the carbon atom next door to the -COOH group.
Amino acids have the general structural molecular formula -NH2CHRCOOH. They have two important functional groups (a functional group means a group of atoms in a molecule that have characteristic chemical reactions regardless of the rest of the molecule): carboxylic acid group -COOH and an amine group -NH2.
Two amino acids can undergo a condensation reaction to form a dipeptide. Further condensation reactions result in a polypeptide. The amino acid units are linked by peptide bonds (sometimes called peptide links).
R1-COOH + R2-NH2 --> R1-CO-NH-R2 + H2O R=a side group.
What else can I help you with?
Which amino acids other than tryptophan display fluorescent emission?
Tyrosine and phenylalanine are two other amino acids that can display fluorescence emission. Tyrosine's fluorescence is typically weaker than tryptophan's, while phenylalanine's fluorescence is even weaker.
Difference between aromatic and aliphatic amino acids?
Aromatic amino acids have a benzene ring in their side chain, which includes phenylalanine, tyrosine, and tryptophan. Aliphatic amino acids have straight or branched hydrocarbon chains in their side chains, which include alanine, valine, leucine, and isoleucine.
What amino acid spreads out in water?
Hydrophilic ("water loving") amino acid side chains are either charged or polar. Both are attracted by water molecules. Histidine, Lysine, Glutamate, Aspartate, Arginine Hydrophobic: Alanine, Isoleucine, Leucine, Phenylalanine, Valine, Proline, Glycine, Methionine, Phenylalanine, Tryptophane, Cysteine. Less Hydrophobic: Tyrosine, Histidine, Serine, Threonine, Proline, Glycine, Alanine, Glutamine
What is the role of sodium borate in the interaction between polyvinyl alcohol and other substances?
Sodium borate, also known as borax, acts as a crosslinking agent in the interaction between polyvinyl alcohol and other substances. It helps to form strong bonds between the polymer chains of polyvinyl alcohol, increasing its strength and stability. This crosslinking process is important in various applications such as adhesives, coatings, and films.
Interaction between individual polypeptide chains to form a protein complex is a what kind of structure?
I'm pretty sure it's quaternary"If several protein chains associate w/ one another to form a functional protein, the protein is said to have a quaternary structure" - 'Human Physiology, 4th E', Dee Unglaub Silverthorn
Which amino acids other than tryptophan display fluorescent emission?
Tyrosine and phenylalanine are two other amino acids that can display fluorescence emission. Tyrosine's fluorescence is typically weaker than tryptophan's, while phenylalanine's fluorescence is even weaker.
Difference between aromatic and aliphatic amino acids?
Aromatic amino acids have a benzene ring in their side chain, which includes phenylalanine, tyrosine, and tryptophan. Aliphatic amino acids have straight or branched hydrocarbon chains in their side chains, which include alanine, valine, leucine, and isoleucine.
What charge to hydrophobic amino acids have at pH6?
Most hydrophobic amino acids like alanine, valine, leucine, isoleucine, phenylalanine, tyrosine, and tryptophan do not have charged side chains at neutral pH (pH 6). Their side chains are usually non-polar, so they do not contribute to any charge on the amino acid at pH 6.
What amino acid spreads out in water?
Hydrophilic ("water loving") amino acid side chains are either charged or polar. Both are attracted by water molecules. Histidine, Lysine, Glutamate, Aspartate, Arginine Hydrophobic: Alanine, Isoleucine, Leucine, Phenylalanine, Valine, Proline, Glycine, Methionine, Phenylalanine, Tryptophane, Cysteine. Less Hydrophobic: Tyrosine, Histidine, Serine, Threonine, Proline, Glycine, Alanine, Glutamine
What amino acids repel water?
Amino acids that repel water are typically hydrophobic, meaning they do not interact favorably with water. Some common hydrophobic amino acids include alanine, valine, leucine, isoleucine, phenylalanine, and tryptophan. These amino acids have nonpolar side chains that make them less soluble in aqueous environments, leading to a tendency to cluster away from water. This characteristic plays a crucial role in protein folding and the formation of membrane structures.
What amino acids are found in cell wall of bacteria?
The cell walls of bacteria primarily contain peptidoglycan, which is composed of sugar chains cross-linked by short peptide segments. The amino acids commonly found in these peptide chains include D-alanine, D-glutamic acid, L-lysine (or meso-diaminopimelic acid in some species), and L-alanine. These amino acids contribute to the structural integrity and rigidity of the bacterial cell wall.
Which of the peptides would absorb light at 280 nm?
Peptides containing aromatic amino acids such as tryptophan, tyrosine, and phenylalanine are known to absorb light at 280 nm. These amino acids are capable of absorbing UV light due to their aromatic side chains, with tryptophan having the highest molar absorptivity at 280 nm.
What is the role of sodium borate in the interaction between polyvinyl alcohol and other substances?
Sodium borate, also known as borax, acts as a crosslinking agent in the interaction between polyvinyl alcohol and other substances. It helps to form strong bonds between the polymer chains of polyvinyl alcohol, increasing its strength and stability. This crosslinking process is important in various applications such as adhesives, coatings, and films.
What level of protein is created by the interaction of multiple polypeptides?
Quaternary structure refers to the level of protein structure that results from the interaction of multiple polypeptide chains. This structure is formed by the association of two or more individual polypeptide chains that come together to form a functional protein complex.
Which of the chains of amino acids corresponds to the nucleotide sequence uca-agc-gua?
Which of the chains of amino acids corresponds to the nucleotide sequence AAUGGCUAC? A. valine-glycine-stop B. methionine-tryptophan-leucine C. isoleucine-arginine-leucine D. asparagine-glycine-tyrosine
A complex interaction between organisms competing for food that may involve several food chains is called?
We just finished studying that last year and i am positive that the answer is food web. Hope that I have been able to help you.
What is foodweb?
A food web links all the food chains in an ecosystem together.
