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Corrigendum to "In vitro and in vivo assessment of a non-animal sourced chitosan scaffold loaded with xeno-free umbilical cord mesenchymal stromal cells cultured under macromolecular crowding conditions" [Biomaterials and Biosystems, Volume 16, December 2024, 100102]. [PDF]

Biomater Biosyst
Nubila AD, Doulgkeroglou MN, Gurdal M, Korntner SH, Zeugolis DI.   +4 more
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Macromolecular crowding: obvious but underappreciated

Trends in Biochemical Sciences, 2001
Biological macromolecules evolve and function within intracellular environments that are crowded with other macromolecules. Crowding results in surprisingly large quantitative effects on both the rates and the equilibria of interactions involving macromolecules, but such interactions are commonly studied outside the cell in uncrowded buffers.
R John Ellis
exaly   +3 more sources

Macromolecular dynamics in crowded environments

The Journal of Chemical Physics, 2010
The structural and dynamical properties of macromolecules in confining or crowded environments are different from those in simple bulk liquids. In this paper, both the conformational and diffusional dynamics of globular polymers are studied in solutions containing fixed spherical obstacles.
Carlos, Echeverria, Raymond, Kapral
openaire   +2 more sources

Macromolecular Crowding and Protein Stability

Journal of the American Chemical Society, 2012
An understanding of cellular chemistry requires knowledge of how crowded environments affect proteins. The influence of crowding on protein stability arises from two phenomena, hard-core repulsions and soft (i.e., chemical) interactions. Most efforts to understand crowding effects on protein stability, however, focus on hard-core repulsions, which are ...
Yaqiang, Wang, Mohona, Sarkar, Austin E, Smith, Alexander S, Krois, Gary J, Pielak   +4 more
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Macromolecular Crowding and Its Consequences

1999
Incompatible pairs of polymers separate into two phases in aqueous solution above a few percentage points total concentration. Protein pairs can also produce phase separation, but at somewhat higher concentrations. In this chapter, we explore the effect of high background concentrations of macromolecules on phase separation of pairs of species which ...
H O, Johansson, D E, Brooks, C A, Haynes
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Activity of Subtilisin Carlsberg in macromolecular crowding

Journal of Photochemistry and Photobiology B: Biology, 2007
Enzymatic activity of a proteolytic enzyme Subtilisin Carlsberg (SC) in anionic sodium dodecyl sulfate (SDS) micellar medium has been explored and found to be retarded compared to that in bulk buffer. Circular dichroism (CD) study reveals that SDS, which is a potential protein denaturant, has an insignificant denaturation effect on SC.
Ajay Kumar, Shaw, Samir Kumar, Pal
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Macromolecular Crowding in Mitochondria

The chapter reviews the various effects of crowding on mitochondrial structure and function. Data illustrate that, as a rule, the concentration of macromolecules in the mitochondrial matrix and inner membrane is at least as high as in other parts of the cytoplasm, while the intermembrane space is sparse.
Semen V, Nesterov, Vladimir N, Uversky
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An early look at macromolecular crowding

Biophysical Chemistry, 1995
Interest in the interaction between proteins and polysaccharides in semidilute systems developed in the late 1950's and early 1960's both in the field of matrix biology and in the construction of new separation techniques. The author gives an account of how his work in the 50's on the characterization of a connective tissue polysaccharide, hyaluronan ...
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Macromolecular crowding: effects on actin polymerisation

Biophysical Chemistry, 1997
Dextran has been found to enhance the polymerisation of actin. This enhancement increases exponentially with increasing mass concentrations of dextran, in a manner that is consistent with excluded volume theory. Mathematical prediction of experimental results is difficult due to the fact that all participating species, namely F-actin, G-actin and ...
R A, Lindner, G B, Ralston
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Macromolecular crowding and molecular recognition

Journal of Molecular Recognition, 1993
AbstractThe effects of macromolecular crowding upon macromolecular associations in solution, and upon binding of a macromolecular ligand to a surface site, ar ereviewed. It is demonstrated, by means of two examples, that crowding may lead to significant alterations of biochemical or biological recognition processes at the molecular level.
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