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Structural biology

About: Structural biology is a research topic. Over the lifetime, 2206 publications have been published within this topic receiving 126070 citations.


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Journal ArticleDOI
TL;DR: A strategy that employs a hybrid surfactant to transfer the protein to the reverse micelle system to solubilize the protein in a low-viscosity solvent and allow for use of standard triple-resonance methods is demonstrated.

40 citations

Journal ArticleDOI
TL;DR: Encapsulation of macromolecules within the protective nanoscale aqueous interior of reverse micelles dissolved in low viscosity fluids has been developed as a means through which the 'slow tumbling problem' can be overcome.

40 citations

Journal ArticleDOI
TL;DR: In vitro studies, incorporating TnTm, suggest that a significant portion of the decreased force and motion during fatigue may be mediated through a disruption of the molecular motions of specific regions within Tn and Tm.
Abstract: The cause of muscle fatigue has been studied for more than 100 yr, yet its molecular basis remains poorly understood. Prevailing theories suggest that much of the fatigue-induced loss in force and velocity can be attributed to the inhibitory action of metabolites, principally phosphate (Pi) and hydrogen ions (H, i.e., acidosis), on the contractile proteins, but the precise detail of how this inhibition occurs has been difficult to visualize at the molecular level. However, recent technological developments in the areas of biophysics, molecular biology, and structural biology are enabling researchers to directly observe the function and dysfunction of muscle contractile proteins at the level of a single molecule. In fact, the first direct evidence that high levels of H and Pi inhibit the function of muscle's molecular motor, myosin, has recently been observed in a single molecule laser trap assay. Likewise, advances in structural biology are taking our understanding further, providing detail at the atomic level of how some metabolites might alter the internal motions of myosin and thereby inhibit its ability to generate force and motion. Finally, new insights are also being gained into the indirect role that muscle regulatory proteins troponin (Tn) and tropomyosin (Tn) play in the fatigue process. In vitro studies, incorporating TnTm, suggest that a significant portion of the decreased force and motion during fatigue may be mediated through a disruption of the molecular motions of specific regions within Tn and Tm. These recent advances are providing unprecedented molecular insight into the structure and function of the contractile proteins and, in the process, are reshaping our understanding of the process of fatigue.

40 citations

Journal ArticleDOI
11 Apr 2017-eLife
TL;DR: Experiments together with molecular modeling using NMR chemical shifts suggest that new interactions involving intrinsically disordered proteins may evolve via a low-affinity complex which is optimized by modulating direct interactions as well as dynamics, while tolerating several potentially disruptive mutations.
Abstract: Proteins are an important building block of life and are vital for almost every process that keeps cells alive. These molecules are made from chains of smaller molecules called amino acids linked together. The specific order of amino acids in a protein determines its shape and structure, which in turn controls what the protein can do. However, a group of proteins called 'intrinsically disordered proteins' are flexible in their shape and lack a stable three-dimensional structure. Yet, these proteins play important roles in many processes that require the protein to interact with a number of other proteins. At multiple time points during evolution, new or modified proteins – and consequently new potential interactions between proteins – have emerged. Often, an interaction that is specific for a group of organisms has evolved a long time ago and not changed since. As intrinsically disordered proteins lack a specific shape, it is harder to study how their structure (or lack of it) influences their purpose; until now, it was not known how their interactions emerge and evolve. Hultqvist et al. analyzed the amino acid sequences of two specific intrinsically disordered proteins from different organisms to reconstruct the versions of the proteins that were likely found in their common ancestors 450-600 million years ago. The ancestral proteins were then ‘resurrected’ by recreating them in test tubes and their characteristics and properties analyzed with experimental and computational biophysical methods. The results showed that the ancestral proteins created weaker bonds between them compared to more ‘modern’ ones, and were more flexible even when bound together. However, once their connection had evolved, the bonds became stronger and were maintained even when the organism diversified into new species. The findings shed light on fundamental principles of how new protein-protein interactions emerge and evolve on a molecular level. This suggests that an originally weak and dynamic interaction is relatively quickly turned into a tighter one by random mutations and natural selection. A next step for the future will be to investigate how other protein-protein interactions have evolved and to identify general underlying patterns. A deeper knowledge of how this molecular evolution happened will broaden our understanding of present day protein-protein interactions and might aid the design of drugs that can mimick proteins.

40 citations

Journal ArticleDOI
28 Nov 2003-Science

40 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202335
202272
2021149
2020154
2019152
2018140