protein Flashcards
primary structure is a chain of amino acid
primary structure is a chain of amino acid
secondary protein structure:
hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern
secondary protein structure:
hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern
teritary protein structure:
three-dimensional folding pattern of a protein due to side chain interactions
teritary protein structure:
three-dimensional folding pattern of a protein due to side chain interactions
quaternary protein structure:
protein consisting of more than one amino acid chain
quaternary protein structure:
protein consisting of more than one amino acid chain
In aβ pleated sheet, _______ segments of a polypeptide chain line up next to each other, forming a sheet-like structure held together by hydrogen bonds. The hydrogen bonds form between ______ and _____ groups of backbone, while the R groups extend above and below the plane of the sheet.
_____ stack
In aβ pleated sheet, two or more segments of a polypeptide chain line up next to each other, forming a sheet-like structure held together by hydrogen bonds. The hydrogen bonds form between carbonyl and amino groups of backbone, while the R groups extend above and below the plane of the sheet
zigzagged stack
In anα helix, the carbonyl (C=O) of one amino acid is hydrogen bonded to the amino H (N-H) of an amino acid that is four down the chain. This pattern of bonding pulls the polypeptide chain into a helical structure that resembles a curled ribbon, with each turn of the helix containing 3.6 amino acids. The R groups of the amino acids stick outward from the α helix, where they are free to interact
rod shaped cyliner
In anα helix, the carbonyl (C=O) of one amino acid is hydrogen bonded to the amino H (N-H) of an amino acid that is four down the chain. This pattern of bonding pulls the polypeptide chain into a helical structure that resembles a curled ribbon, with each turn of the helix containing 3.6 amino acids. The R groups of the amino acids stick outward from the α helix, where they are free to interact
______ (size-fit in small spaces, covalent bond,flexible,free rotation around alpha carbon)
______ (shape-kink, form a second covalent bond with the backbone)
______ (S-S bond formation, kink back bond, bond back to the side chain, disulphur)
proline (secondary alpha amino group)
Glycine (size-fit in small spaces, covalent bond,flexible,free rotation around alpha carbon)
Proline (shape-kink, form a second covalent bond with the backbone)
Cysteine (S-S bond formation, kink back bond, bond back to the side chain, disulphur)
proline (secondary alpha amino group)
The nonpolar (hydrophobic) side chains tend to __________ of the folded protein (just as hydrophobic oil droplets coalesce to form one large drop).
The nonpolar (hydrophobic) side chains tend to cluster in the interior of the folded protein (just as hydro- phobic oil droplets coalesce to form one large drop).
\_\_\_\_\_\_ protein (filament) \_\_\_\_\_\_ protein (machinery, catalyst reaction)
Fibrous protein (filament) Globular protein (machinery, catalyst reaction)
in an aqueous environment, hydro- phobic molecules, including the nonpolar side chains of particular amino acids, tend to be forced together to minimize their disruptive effect on the hydrogen-bonded network of the surrounding water molecules
in an aqueous environment, hydro- phobic molecules, including the nonpolar side chains of particular amino acids, tend to be forced together to minimize their disruptive effect on the hydrogen-bonded network of the surrounding water molecules
In contrast, polar side chains tend to arrange themselves near the outside of the folded protein, where they can form hydrogen bonds with water and with other polar mole- cules
In contrast, polar side chains tend to arrange themselves near the outside of the folded protein, where they can form hydrogen bonds with water and with other polar mole- cules
A protein domain usually contains between 40 and 350 amino acids—folded into α helices and β sheets and other elements of secondary structure—and it is the modu- lar unit from which many larger proteins are constructed
A protein domain usually contains between 40 and 350 amino acids—folded into α helices and β sheets and other elements of secondary structure—and it is the modu- lar unit from which many larger proteins are constructed
In an α helix and in the central strands
of a β sheet, all of the ____ and _____ groups in the polypeptide backbone are engaged in hydrogen bonds. This gives considerable stability to these secondary structural elements, and it allows them to form in many different proteins.
In an α helix and in the central strands
of a β sheet, all of the N–H and C=O groups in the polypeptide backbone are engaged in hydrogen bonds. This gives considerable stability to these secondary structural elements, and it allows them to form in many different proteins.
The heat-inactivation of the enzyme suggests that the mutation causes the enzyme to have a less stable structure. For example, a hydrogen bond that is normally formed between two amino acid side chains might no longer be formed because the mutation replaces one of these amino acids with a different one that cannot participate in the bond.
The heat-inactivation of the enzyme suggests that the mutation causes the enzyme to have a less stable structure. For example, a hydrogen bond that is normally formed between two amino acid side chains might no longer be formed because the mutation replaces one of these amino acids with a different one that cannot participate in the bond.
beta turns contain 4 _______ and are stabilized by hydrogen bonding between the carboxyl oxygen of the first residue and the amide hydrogen of the fourth residue
beta turns contain 4 amino acid residues and are stabilized by hydrogen bonding between the carboxyl oxygen of the first residue and the amide hydrogen of the fourth residue
