Insight into polyproline II helical bundle stability in an antifreeze protein denatured state

Treviño, Miguel Á.; Sánchez, Rubén López; Moya, María Redondo; Pantoja-Uceda, David; Mompeán, Miguel; Laurents, Douglas V.

doi:10.1016/j.bpj.2022.10.034

Cited by 4 publications

(2 citation statements)

References 44 publications

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“…In particular, the antifreeze proteins have proven valuable as systems to investigate the bases of the conformational stability of glycine-rich PPII helical bundles and have revealed disulfide bonds, nonconventional Cα-H•••O=C hydrogen bonds, and a lower than anticipated conformational entropy in the denatured state as factors favoring the folded structure 20,21,22 . Nevertheless, some important questions remain regarding the roles of : 1) flanking sequences, which are known to be important for amyloid structures 23 , 2) packing density, which is expected to impact the stabilizing contribution of van der Waals interactions, 3) the parallel versus antiparallel orientation of the helices 10 , which we hypothesize could be stabilizing or destabilizing due to macrodipole interactions and 4) unconventional Cα-H•••O=C hydrogen bonds.…”

Section: Introductionmentioning

confidence: 99%

Architectonic principles of polyproline II helix bundle protein domains

Rodríguez,

Laurents

2024

Archives of Biochemistry and Biophysics

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Section: Introductionmentioning

confidence: 99%

Architectonic principles of polyproline II helix bundle protein domains

Rodríguez,

Laurents

2024

Archives of Biochemistry and Biophysics

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“…In particular, the antifreeze proteins have proven valuable as systems to investigate the bases of the conformational stability of glycine-rich PPII helical bundles and have revealed disulfide bonds, nonconventional Cα-H···O=C hydrogen bonds, and a lower than anticipated conformational entropy in the denatured state as factors favoring the folded structure 66,35,67 . Nevertheless, some important questions remain regarding the roles of : 1) flanking sequences, which are known to be important for amyloid structures 68 , 2) packing density, which is expected to impact the stabilizing contribution of van der Waals interactions, 3) the parallel versus antiparallel orientation of the helices 53 , which we hypothesize could be stabilizing or destabilizing due to macrodipole interactions and 4) unconventional Cα-H···O=C hydrogen bonds.…”

Section: Introductionmentioning

confidence: 99%

Architectonic Principles of Polyproline II Helix Bundle Protein Domains

Rodríguez,

Laurents

2023

Preprint

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Glycine rich polyproline II helix assemblies are an emerging class of natural domains found in several proteins with different functions and diverse origins. The distinct properties of these domains relative to those composed of α-helices and β-sheets could make glycine-rich polyproline II helix assemblies a useful building block for protein design. However, the architectonic bases of these structures are not well known. Here, we compare and analyze their structures to uncover common features. These protein domains are found to be highly tolerant of distinct flanking sequences. This speaks to the robustness of this fold and strongly suggests that glycine rich polyproline II assemblies could be grafted with other protein domains to engineer new structures and functions. These domains are also well packed with few or no cavities. Moreover, a significant trend towards anti-parallel helix configuration is observed in all these domains and could provide stabilizing interactions among macrodipoles. Finally, extensive networks of Cα-H···O=C hydrogen bonds are detected in these domains. Despite their diverse evolutionary origins and activities, glycine-rich polyproline II helix assemblies share architectonic features which could help guide the design of novel proteins.

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Nuclear spin relaxation

Kowalewski

2023

Nuclear Magnetic Resonance

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This review covers the progress in the field of NMR relaxation in fluids during 2022. The emphasis is on comparatively simple liquids and solutions of physico-chemical and chemical interest, in analogy with the previous periods, but selected biophysics-related topics (here, I also include some work on relaxation in solid biomaterials) and relaxation-related studies on more complex systems (macromolecular solutions, liquid crystalline systems, glassy and porous materials) are also covered. Section 2 of the chapter is concerned with general, physical and experimental aspects of nuclear spin relaxation, while Section 3 is concentrated on applications.

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Insight into polyproline II helical bundle stability in an antifreeze protein denatured state

Cited by 4 publications

References 44 publications

Architectonic principles of polyproline II helix bundle protein domains

Architectonic principles of polyproline II helix bundle protein domains

Architectonic Principles of Polyproline II Helix Bundle Protein Domains

Nuclear spin relaxation

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