explain the hydrogen bonding pattern for B sheet ( parallel and antiparallel, alpha helix and B...
Homework Answers
The alpha helix is the major structural element in proteins.In helix,the carbonyl oxygen atoms C=O point in one direction,towards the amide NH groups 4 residues away (I,I+4).Together these groups form a hydrogen bond ,one of the main forces in stabilisation of secondary structure in proteins.
The B sheet consists of several B strands ,stretched segments of the polypeptide chain kept together by a network of H-bonds.Each B strands is represented by an arrow,which defines it's direction starting from the N-terminus to the C-terminus.When the strand arrows point in the same direction ,the sheet is parallel
When the strand arrows point in opposite direction ,the sheet is anti-parallel
.
alpha
sheet 
B sheet 
B sheet parallel
B sheet antiparallel
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explain the hydrogen bonding pattern for B sheet ( parallel and
antiparallel, alpha helix and B...
Which interaction holds the a-helix and the B-pleated sheet into its unique folding pattern? hydrogen bonding...
Which interaction holds the a-helix and the B-pleated sheet into its unique folding pattern? hydrogen bonding between nitrogens and oxygens in the polypeptide backbone hydrogen bonding between serines (-CH2OH) covalent bonding between cysteines (-CH2SH) ionic bonding between acidic and basic amino acid side chains hydrophilic interactions
Question 1 (Mandatory) (1 point) The following is an example of_ H-N a parallel alpha-helix a...
Question 1 (Mandatory) (1 point) The following is an example of_ H-N a parallel alpha-helix a parallel beta-sheet an antiparallel alpha-helix an antiparallel beta-sheet ● a domain
Sort each peptide chain as part of a parallel fi sheet, part of an antiparallel beta...
Sort each peptide chain as part of a parallel fi sheet, part of an antiparallel beta sheet, either (cannot determine if parallel or antiparallel), or not part of a fi sheet (for example, if it is part of an alpha helix). Be as specific as possible. For example, if a given structure is a parallel fi sheet, identify it as such.
Question 19 1pts contain hydrogen bonds between parallel or antiparallel or a combination of parallel and...
Question 19 1pts contain hydrogen bonds between parallel or antiparallel or a combination of parallel and antiparallel. Beta-sheets Alpha-helices Neither Alpha-helices nor Beta-sheets o Both Alpha-helices and Beta-sheets
22. Consider an alpha helix with sequence VLADWMAVELA, and consider the hydrogen bonds that are required in order to fo...
22. Consider an alpha helix with sequence VLADWMAVELA, and consider the hydrogen bonds that are required in order to form the alpha helix. A. Fill in all of the hydrogen bonds that must form between a given residue's backbone N-H backbone C-O, or R group, indicating what the hydrogen bonding partner for each will be. For example, the C-O of V1 is a hydrogen bond acceptor of the W5 N-H hydrogen bond donor, reflected in the appropriate squares under V1...
22. Consider an alpha helix with sequence VLADWMAVELA, and consider the hydrogen bonds that are required in order to fo...
22. Consider an alpha helix with sequence VLADWMAVELA, and consider the hydrogen bonds that are required in order to form the alpha helix. A. Fill in all of the hydrogen bonds that must form between a given residue's backbone N-H backbone C-O, or R group, indicating what the hydrogen bonding partner for each will be. For example, the C-O of V1 is a hydrogen bond acceptor of the W5 N-H hydrogen bond donor, reflected in the appropriate squares under V1...
Part A Which is not true about beta-sheets? Antiparallel sheets provide better hydrogen bonding than parallel...
Part A Which is not true about beta-sheets? Antiparallel sheets provide better hydrogen bonding than parallel sheets Antiparallel is when two peptide strands run in opposite directions The sheets are pleated The side chain of the residues are side-by-side (planar) to the peptide backbone
Sort each peptide chain as part of a parallel %u03B2 sheet, part of an antiparallel %u03B2...
Sort each peptide chain as part of a parallel %u03B2 sheet, part of
an antiparallel %u03B2 sheet, either (cannot determine if parallel
or antiparallel), or not part of a %u03B2 sheet (for example, if it
is part of an %u03B1 helix). Be as specific as possible. For
example, if a given structure is a parallel %u03B2 sheet, identify
it as such.
There are four amino acid residues between each turn of an alpha helix, because O hydrogen...
There are four amino acid residues between each turn of an alpha helix, because O hydrogen bonding between the carbonyl and amine groups is more stable at this distance. O amino acid residues need a certain amount of distance between then during the turn. O the polar amino acids are more attractive to the peptide bond at this distance. O None of the choices are correct.
Part A Which is not true about beta-sheets? O Antiparallel sheets provide better hydrogen bonding than...
Part A Which is not true about beta-sheets? O Antiparallel sheets provide better hydrogen bonding than parallel sheets O Antiparallel is when two peptide strands run in opposite directions. O The sheets are pleated The side chain of the residues are side-byside (planar) to the peptide backbone. Submit Request Answer
Which interaction holds the a-helix and the B-pleated sheet into its unique folding pattern? hydrogen bonding between nitrogens and oxygens in the polypeptide backbone hydrogen bonding between serines (-CH2OH) covalent bonding between cysteines (-CH2SH) ionic bonding between acidic and basic amino acid side chains hydrophilic interactions
Question 1 (Mandatory) (1 point) The following is an example of_ H-N a parallel alpha-helix a parallel beta-sheet an antiparallel alpha-helix an antiparallel beta-sheet ● a domain
Sort each peptide chain as part of a parallel fi sheet, part of an antiparallel beta sheet, either (cannot determine if parallel or antiparallel), or not part of a fi sheet (for example, if it is part of an alpha helix). Be as specific as possible. For example, if a given structure is a parallel fi sheet, identify it as such.
Question 19 1pts contain hydrogen bonds between parallel or antiparallel or a combination of parallel and antiparallel. Beta-sheets Alpha-helices Neither Alpha-helices nor Beta-sheets o Both Alpha-helices and Beta-sheets
22. Consider an alpha helix with sequence VLADWMAVELA, and consider the hydrogen bonds that are required in order to form the alpha helix. A. Fill in all of the hydrogen bonds that must form between a given residue's backbone N-H backbone C-O, or R group, indicating what the hydrogen bonding partner for each will be. For example, the C-O of V1 is a hydrogen bond acceptor of the W5 N-H hydrogen bond donor, reflected in the appropriate squares under V1...
22. Consider an alpha helix with sequence VLADWMAVELA, and consider the hydrogen bonds that are required in order to form the alpha helix. A. Fill in all of the hydrogen bonds that must form between a given residue's backbone N-H backbone C-O, or R group, indicating what the hydrogen bonding partner for each will be. For example, the C-O of V1 is a hydrogen bond acceptor of the W5 N-H hydrogen bond donor, reflected in the appropriate squares under V1...
Part A Which is not true about beta-sheets? Antiparallel sheets provide better hydrogen bonding than parallel sheets Antiparallel is when two peptide strands run in opposite directions The sheets are pleated The side chain of the residues are side-by-side (planar) to the peptide backbone
Sort each peptide chain as part of a parallel %u03B2 sheet, part of
an antiparallel %u03B2 sheet, either (cannot determine if parallel
or antiparallel), or not part of a %u03B2 sheet (for example, if it
is part of an %u03B1 helix). Be as specific as possible. For
example, if a given structure is a parallel %u03B2 sheet, identify
it as such.
There are four amino acid residues between each turn of an alpha helix, because O hydrogen bonding between the carbonyl and amine groups is more stable at this distance. O amino acid residues need a certain amount of distance between then during the turn. O the polar amino acids are more attractive to the peptide bond at this distance. O None of the choices are correct.
Part A Which is not true about beta-sheets? O Antiparallel sheets provide better hydrogen bonding than parallel sheets O Antiparallel is when two peptide strands run in opposite directions. O The sheets are pleated The side chain of the residues are side-byside (planar) to the peptide backbone. Submit Request Answer
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