Observation of the Glycines in Elastin Using <sup>13</sup>C and <sup>15</sup>N Solid-State NMR Spectroscopy and Isotopic Labeling

Perry, Ashlee; Stypa, Michael P.; Foster, Jeffrey S.; Kumashiro, Kristin K.

doi:10.1021/ja017711x

Cited by 30 publications

(56 citation statements)

References 25 publications

(62 reference statements)

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“…Also, a systematic study of elastin as a function of temperature and hydration using 13 C NMR evidenced a stepwise increase of mobility in this fiber when hydrated at .40% (106). In addition, highly mobile glycine residues could be resolved in two different environments (113). The comparison of 13 C CP and DP spectra also allowed observing a similar stepwise behavior upon hydration in an elastin model compound (105).…”

Section: Signal Intensity Line Width and Line Shape Analysismentioning

confidence: 66%

“…In amyloid fibers, typical half-height widths of 13 C resonances are about 1.5-2.5 ppm; broader lines indicate conformational disorder whereas sharper ones are indicative of motional narrowing or an unusually high degree of structural order (114). On the other hand, reported 13 C line widths in structural fibers are $6.5 ppm for carbonyllabeled alanines in silk (115), $4-6 ppm for carbonyl groups in wool keratin (56), $2 ppm for glycine carbonyls in elastin (113), and up to $10 ppm for the sum of carbonyl peaks in natural-abundance elastin (106). These values reflect the high degree of conformational disorder characteristic of natural fibers.…”

Section: Signal Intensity Line Width and Line Shape Analysismentioning

confidence: 99%

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Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Arnold

Marcotte

2009

Concepts Magnetic Resonance

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As a consequence of evolutionary pressure, various organisms have developed structural fibers displaying a range of exceptional mechanical properties adapted specifically to their functions. An understanding of these properties at the molecular level requires a detailed description of local structure, orientation with respect to the fiber and size of constitutive units, and dynamics on various timescales. The size and lack of long-range order in these protein systems constitute an important challenge to classical structural techniques such as high-resolution NMR and X-ray diffraction. Solidstate NMR overcomes these constraints and is uniquely suited to the study of these inherently disordered systems. Solid-state NMR experiments developed or applied to determine structure, orientation, and dynamics of these complex proteins will be reviewed and illustrated through examples of their applications to fibers such as spider and silkworm silks, collagen, elastin, and keratin.

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Section: Signal Intensity Line Width and Line Shape Analysismentioning

confidence: 66%

Section: Signal Intensity Line Width and Line Shape Analysismentioning

confidence: 99%

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Arnold

Marcotte

2009

Concepts Magnetic Resonance

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“…138 The major biological function of elastin relies on its ability to elastically extend and contract in repetitive motion when hydrated. [139][140][141][142][143] Although monomers of elastin are highly disordered, random coil-like polypeptides, 138,[144][145][146][147] because of the formation of the elastic supramolecular complexes, this protein has been shown to be one of the longest lasting proteins in the body, possessing a half-life of about 74 y. 148 …”

Section: Making Sturdy Complexesmentioning

confidence: 99%

Paradoxes and wonders of intrinsic disorder: Stability of instability

Uversky

2017

Intrinsically Disordered Proteins

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This article continues a series of short comments on the paradoxes and wonders of the protein intrinsic disorder phenomenon by introducing the "stability of instability" paradox. Intrinsically disordered proteins (IDPs) are characterized by the lack of stable 3D-structure, and, as a result, have an exceptional ability to sustain exposure to extremely harsh environmental conditions (an illustration of the "you cannot break what is already broken" principle). Extended IDPs are known to possess extreme thermal and acid stability and are able either to keep their functionality under these extreme conditions or to rapidly regain their functionality after returning to the normal conditions. Furthermore, sturdiness of intrinsic disorder and its capability to "ignore" harsh conditions provides some interesting and important advantages to its carriers, at the molecular (e.g., the cell wall-anchored accumulation-associated protein playing a crucial role in intercellular adhesion within the biofilm of Staphylococcus epidermidis), supramolecular (e.g., protein complexes, biologic liquid-liquid phase transitions, and proteinaceous membrane-less organelles), and organismal levels (e.g., the recently popularized case of the microscopic animals, tardigrades, or water bears, that use intrinsically disordered proteins to survive desiccation).

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“…Elastin resilience is afforded by the formation of insoluble fibers, the first step of which involves the selfalignment of elastin monomers, tropoelastin, in a temperature-induced transition known as coacervation, through the association of hydrophobic domains (1,2). Although highly (Ͼ75%) non-polar in character, tropoelastin remains predominantly monomeric and structurally disordered in solution (3)(4)(5) and critically, retains substantial backbone hydration and flexibility even when assembled (6) and cross-linked into mature, polymeric elastic arrays (7)(8)(9)(10)(11)(12)(13).…”

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confidence: 99%

Proline Periodicity Modulates the Self-assembly Properties of Elastin-like Polypeptides

Muiznieks

Keeley

2010

Journal of Biological Chemistry

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Elastin is a self-assembling protein of the extracellular matrix that provides tissues with elastic extensibility and recoil. The monomeric precursor, tropoelastin, is highly hydrophobic yet remains substantially disordered and flexible in solution, due in large part to a high combined threshold of proline and glycine residues within hydrophobic sequences. In fact, proline-poor elastin-like sequences are known to form amyloidlike fibrils, rich in ␤-structure, from solution. On this basis, it is clear that hydrophobic elastin sequences are in general optimized to avoid an amyloid fate. However, a small number of hydrophobic domains near the C terminus of tropoelastin are substantially depleted of proline residues. Here we investigated the specific contribution of proline number and spacing to the structure and self-assembly propensities of elastin-like polypeptides. Increasing the spacing between proline residues significantly decreased the ability of polypeptides to reversibly self-associate. Real-time imaging of the assembly process revealed the presence of smaller colloidal droplets that displayed enhanced propensity to cluster into dense networks. Structural characterization showed that these aggregates were enriched in ␤-structure but unable to bind thioflavin-T. These data strongly support a model where proline-poor regions of the elastin monomer provide a unique contribution to assembly and suggest a role for localized ␤-sheet in mediating self-assembly interactions.Elastin is the extracellular matrix protein responsible for the elasticity of vertebrate arterial vessels, connective tissues, lung, and skin. Elastin resilience is afforded by the formation of insoluble fibers, the first step of which involves the selfalignment of elastin monomers, tropoelastin, in a temperature-induced transition known as coacervation, through the association of hydrophobic domains (1, 2). Although highly (Ͼ75%) non-polar in character, tropoelastin remains predominantly monomeric and structurally disordered in solution (3-5) and critically, retains substantial backbone hydration and flexibility even when assembled (6) and cross-linked into mature, polymeric elastic arrays (7-13).Maintenance of structural heterogeneity and dynamics of the elastin backbone is achieved in large part by a high proportional composition of both proline (14%) and glycine (35%) residues within hydrophobic sequences (6, 14). These residues are commonly arranged into repeated motifs based on recurring sequence elements such as PGV and GVA. This includes a seven-fold tandem PGVGVA repeat in domain 24 of the native human elastin sequence (15). Contrary to enhancing coacervation or elastomeric properties, the multiple substitution of glycine residues for prolines within tandem repeat sequences (e.g. PGVGVA to GGVGVA) results in the formation of amyloid-like fibrils, rich in ␤-structure, from solution (6, 14). These structures are conformationally more restricted than native elastomeric sequences as a result of the tighter packing of residues into extended...

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Observation of the Glycines in Elastin Using ¹³C and ¹⁵N Solid-State NMR Spectroscopy and Isotopic Labeling

Cited by 30 publications

References 25 publications

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Paradoxes and wonders of intrinsic disorder: Stability of instability

Proline Periodicity Modulates the Self-assembly Properties of Elastin-like Polypeptides

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Observation of the Glycines in Elastin Using 13C and 15N Solid-State NMR Spectroscopy and Isotopic Labeling

Cited by 30 publications

References 25 publications

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Studying natural structural protein fibers by solid‐state nuclear magnetic resonance

Paradoxes and wonders of intrinsic disorder: Stability of instability

Proline Periodicity Modulates the Self-assembly Properties of Elastin-like Polypeptides

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Product

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Observation of the Glycines in Elastin Using ¹³C and ¹⁵N Solid-State NMR Spectroscopy and Isotopic Labeling