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Help with peptide sequencing!?

Help with peptide sequencing!? - Peptide Forum

Help with peptide sequencing!? - Peptide Forum. Ask and discuss questions on peptide protocols, custom peptide synthesis, peptide identification and peptide sequencing.


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Old 02-13-2012, 03:17 PM
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Default Help with peptide sequencing!?



Which of the following peptides is more likely to take up an ?-helical structure and why?

i. LKAENDEAARAMSEA
ii. CRAGGFPWDQPGTSN

amino acidthree letter codesingle letter code
glycine GlyG
alanine AlaA
valine ValV
leucine LeuL
isoleucine IleI
methionine MetM
phenylalanine PheF
tryptophan TrpW
proline ProP

serine SerS
threonine ThrT
cysteine CysC
tyrosine TyrY
asparagine AsnN
glutamine GlnQ

aspartic acid AspD
glutamic acid GluE

lysine LysK
arginine ArgR
histidine HisH
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Old 06-13-2012, 04:15 AM
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Smile Re: Help with peptide sequencing!?

An alpha-helix is a right-handed coil of amino-acid residues on a polypeptide chain. This coil is held together by hydrogen bonds between the oxygen of C=O on top coil and the hydrogen of N-H on the bottom coil. Such a hydrogen bond is formed exactly every 4 amino acid residues, and every complete turn of the helix is only 3.6 amino acid residues. This regular pattern gives the alpha-helix very definite features with regards to the thickness of the coil and the length of each complete turn along the helix axis.

The structural integrity of an alpha-helix is in part dependent on correct steric configuration. Amino acids whose R-groups are too large (tryptophan, tyrosine) or too small (glycine) destabilize alpha-helices. Proline also destabilizes alpha-helices because of its irregular geometry; its R-group bonds back to the nitrogen of the amide group, which causes steric hindrance.

Thus from above two peptide
i. LKAENDEAARAMSEA more likely to take up an alpha-helical structure,

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Kunal pandya
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