Measurements of the molecular weight of (Pro-Pro-Gly), and (Pro-Pro-Gly),(Ala-Pro-Gly),(Pro-Pro-Gly),, which were synthesized by the solid-phase method, revealed that they formed a trimer in an aqueous solution, and dissociated into single-stranded chains on warming. Accompanying the transition, a l
The formation of the triple helix in a mixed solution of (Pro-Pro-Gly)n and (Pro-Pro-Gly)n′. A model of molecular size recognition
✍ Scribed by Yukio Suezaki; Nobuhiro Gō
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1974
- Tongue
- English
- Weight
- 465 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
A theoretical analysis is given of the triple‐helix–random‐coil transition in a mixed solution of poly(Pro‐Pro‐Gly)~n~ with two different but defined degrees of polymerization n and n′. Because of the highly cooperative nature of this helix–coil transition, each polypeptide chain tends to form a triple helix with other polypeptide chains with the same degree of polymerization (size recognition). Occurrence of triple helices consisting of polypeptide chains with different degrees of polymerization (error in recognition) is studied in detail as a function of the cooperativity, and n and n′. Implication of this analysis for molecular recognition in general is discussed.
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## Abstract Interpreting the data of Kobayashi et al.^1^ on the thermal transitions of triple helices of (gly‐pro‐pro)~__n__~ for __n__ = 10, 15, and 20 using a simple model of unzippering and chain dissociation, the thermodynamic parameters characterizing gly‐pro‐pro triple‐helix formation have be
## Abstract The kinetic curves of the helix‐refolding of (PPG)~__n__~ (__n__ = 10, 12, and 15) were analyzed with an all‐or‐none model. The Arrhenius plot of the overall rate constant of the helixfolding __k__~__F__~ showed a negative activation energy at high temperature. With the aid of a sequent
## Abstract The properties of triple‐helix formation of (Pro‐Pro‐Gly)~__n__~ were studied. The probability of hybridization between the polytripeptides (Pro‐Pro‐Gly)~__n__~, of different degrees of polymerization was investigated by gel filtrations of mixed solutions of them. Using samples selectiv
## Abstract Pro–Hyp–Gly is a characteristic amino acid sequence found in fibrous collagens, and (Pro–Hyp–Gly)~10~, which has been widely used as a collagen‐model peptide, forms a stable triple‐helical structure. Here, we synthesized polypeptides consisting of the Pro–Hyp–Gly sequence by direct poly