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Updated: Aug 24, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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振动拉曼光学活动的特征 聚 (l-proline) II螺旋在氨酸寡中

Iain H McColl1, Ewan W Blanch, Lutz Hecht

  • 1Department of Chemistry, University of Glasgow, U.K.

Journal of the American Chemical Society
|April 22, 2004
PubMed
概括

振动拉曼光学活性 (ROA) 光谱显示,水中的氨酸采用了聚-1-二烯 (PPII) 螺旋结构. 这项研究证实了PPII形状的ROA频段分配,有助于蛋白质折叠研究.

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Protein Organization01:13

Protein Organization

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Protein Organization

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NMR Spectroscopy Of Amines

In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is broad and...
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Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
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¹H NMR of Labile Protons: Temporal Resolution

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