NMR studies of flexible peptides in cavities mimicking the synaptic cleft

Pavone, Luca; Crescenzi, Orlando; Tancredi, Teodorico; Temussi, Piero Andrea

doi:10.1016/s0014-5793(02)02336-0

Cited by 8 publications

(6 citation statements)

References 17 publications

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“…34 The same indication came, indirectly, by the increase in the size of NOEs of a small peptide (enkephalin) when measured in PAG, with respect to the corresponding values in bulk. 40 In addition, the pores have an irregular shape that originates from the intricate mesh of polymer fibers, resembling to …”

Section: Discussionmentioning

confidence: 99%

Protein Stability in Nanocages: A Novel Approach for Influencing Protein Stability by Molecular Confinement

Bolis

Politou

Kelly

et al. 2004

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 99%

Protein Stability in Nanocages: A Novel Approach for Influencing Protein Stability by Molecular Confinement

Bolis

Politou

Kelly

et al. 2004

Journal of Molecular Biology

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“…The effect of crowding and confinement was only recently identified as an important property of the cell and its compartments that has been neglected for a long time. As far as bioactive peptides are concerned, it was shown that confinement in a polyacrylamide gel can induce some conformational ordering in enkephalin . The corresponding structure‐inducing influence on the IUPs seems less pronounced but it is in order to remark that this approach is still in its infancy.…”

Section: Towards Iups and Beyond: New Tools To Characterize Flexible ...mentioning

confidence: 99%

“…As far as bioactive peptides are concerned, it was shown that confinement in a polyacrylamide gel can induce some conformational ordering in enkephalin. 58 The corresponding structure-inducing influence on the IUPs seems less pronounced 59 but it is in order to remark that this approach is still in its infancy.…”

Section: Towards Iups and Beyond: New Tools To Characterize Flexible ...mentioning

confidence: 99%

When “IUPs” were “BAPs”: How to study the nonconformation of intrinsically unfolded polyaminoacid chains

Pastore¹,

Temussi

2013

Biopolymers

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Ideas often recur. It has been pointed out recently that proteins are not always the well-structured entities we have become accustomed to from crystallographic studies, but may be intrinsically unstructured or contain unstructured regions. This feature, far from making these proteins less interesting, is an essential requirement for their function. Fascinating though it may be, the concept of so-called intrinsically unfolded (or unordered) proteins (IUPs), also often referred to as intrinsically disordered proteins (IDPs), is not new: it directly links back to the 1970s when the attention of many structural biologists was focused on biologically active peptides, which like IUPs lack a specific defined conformation. The recurrent nature of this concept may now be of topical interest since it suggests the transfer, upon suitable adaptation, of old tools to develop new ideas. Here, we review some of the approaches that were developed for the study of peptides and discuss how they could inspire powerful new methodologies for the study of IUPs.

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“…obtained by means of a capillary flow technique is 6 times higher than that of room temperature water. [269,[272][273][274][275] To date, several NMR studies have involved supercooled water without addition of cryosolvent, either at atmospheric pressure in micro-emulsions (or reverse micelles), [276][277][278][279][280][281][282][283] in glass capillary tubes, [283][284][285][286][287][288][289][290][291][292][293][294][295][296][297][298] and in polymer gels, [299][300][301][302] or at high pressure by means of suitable NMR equipment (see section 2.11) [269, 303-312]…”

Section: Phosphoric Acid-d3 (H3po4-d3)mentioning

confidence: 99%

“…explored. Pastore et al posited that confinement of NPS in agarose gel might induce some degree of folding, as observed for enkephalin in PAG [299]. They investigated [Ala]20 NPS in agarose gel at two different concentrations (1.5% and 4%) and with addition of a crowding agent, at low temperature, and in bulk water, at room temperature.…”

mentioning

confidence: 99%

Tailoring the nuclear Overhauser effect for the study of small and medium-sized molecules by solvent viscosity manipulation

Lameiras

2021

Progress in Nuclear Magnetic Resonance Spectroscopy

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The nuclear Overhauser effect (NOE) is a consequence of cross-relaxation between nuclear spins mediated by dipolar coupling. Its sensitivity to internuclear distances has made it an increasingly important tool for the determination of throughspace atom proximity relationships within molecules of sizes ranging from the smallest systems to large biopolymers. With the support of sophisticated FT-NMR techniques, the NOE plays an essential role in structure elucidation, conformational and dynamic investigations in liquid-state NMR. The efficiency of magnetization transfer by the NOE depends on the molecular rotational correlation time, whose value depends on solution viscosity. The magnitude of the NOE between 1 H nuclei varies from +50 % when molecular tumbling is fast to -100% when it is slow, the latter case corresponding to the spin diffusion limit.In an intermediate tumbling regime, the NOE may be vanishingly small. Increasing the viscosity of the solution increases the motional correlation time, and as a result, otherwise unobservable NOEs may be revealed and brought close to the spin diffusion limit. The goal of this review is to report the resolution of structural problems that benefited from the manipulation of the negative NOE by means of viscous solvents, including examples of molecular structure determination, conformation elucidation and mixture analysis (the ViscY method).3.7. Overview of advantages/disadvantages of viscous solvents in molecule mixture analysis 68 Conclusion 71Acknowledgements References 71Glossary 82

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NMR studies of flexible peptides in cavities mimicking the synaptic cleft

Cited by 8 publications

References 17 publications

Protein Stability in Nanocages: A Novel Approach for Influencing Protein Stability by Molecular Confinement

Protein Stability in Nanocages: A Novel Approach for Influencing Protein Stability by Molecular Confinement

When “IUPs” were “BAPs”: How to study the nonconformation of intrinsically unfolded polyaminoacid chains

Tailoring the nuclear Overhauser effect for the study of small and medium-sized molecules by solvent viscosity manipulation

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