On the split personality of penultimate proline.
On the split personality of penultimate proline.
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DOI：
10.1007/s13361-014-1049-y
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发表时间：
2015-03
影响因子：
3.2
通讯作者：
Clemmer DE
中科院分区：
文献类型：
--
作者：
Glover MS;Shi L;Fuller DR;Arnold RJ;Radivojac P;Clemmer DE
通过离子迁移谱-质谱（IMS-MS）、氨基酸取代和分子建模的组合来检查多肽序列中氨基酸脯氨酸的位置的影响。结果表明，当脯氨酸作为N-末端的第二个残基存在时（即，倒数第二脯氨酸），形成两个构象异构体家族。我们证明了这些家庭的存在，通过研究一系列的截短和突变的肽来自11个残基的肽Ser 1-Pro2-Glu 3-Leu 4-Pro5-Ser 6-Pro7-Gln 8-Ala 9-Glu 10-Lys 11。我们发现，每个肽从这个序列与倒数第二脯氨酸残基具有多种构象。Ala取代Pro残基表明，由于Xaa 1-Pro 2肽键不太可能采用顺式异构体，因此Xaa 1-Ala肽键的顺式-反式异构化产生了多种构象异构体，并且对58种肽的文库的光谱检查表明，约80%的序列显示出这种效应。一个简单的机制，表明顺式和反式脯氨酸形式之间的障碍是降低，因为低的空间阻抗提出。这一观察结果也可能具有有趣的生物学意义，我们注意到许多生物活性肽具有倒数第二个脯氨酸残基。
The influence of the position of the amino acid proline in polypeptide sequences is examined by a combination of ion mobility spectrometry-mass spectrometry (IMS-MS), amino acid substitutions, and molecular modeling. The results suggest that when proline exists as the second residue from the N-terminus (i.e., penultimate proline), two families of conformers are formed. We demonstrate the existence of these families by a study of a series of truncated and mutated peptides derived from the 11-residue peptide Ser1-Pro2-Glu3-Leu4-Pro5-Ser6-Pro7-Gln8-Ala9-Glu10-Lys11. We find that every peptide from this sequence with a penultimate proline residue has multiple conformations. Substitution of Ala for Pro residues indicates that multiple conformers arise from the cis- trans isomerization of Xaa1–Pro2 peptide bonds as Xaa–Ala peptide bonds are unlikely to adopt the cis isomer, and examination of spectra from a library of 58 peptides indicates that ~80% of sequences show this effect. A simple mechanism suggesting that the barrier between the cis-and trans-proline forms is lowered because of low steric impedance is proposed. This observation may have interesting biological implications as well, and we note that a number of biologically active peptides have penultimate proline residues.
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