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Journal articles on the topic 'Proteins crowding'

Author: Grafiati

Published: 10 March 2023

Last updated: 31 July 2025

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1

Zhou, Huan-Xiang. "Crowding Effects of Membrane Proteins." Journal of Physical Chemistry B 113, no. 23 (2009): 7995–8005. http://dx.doi.org/10.1021/jp8107446.

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2

Rhoades, Elizabeth. "Proteins: Disorder, Folding, and Crowding." Biophysical Journal 117, no. 1 (2019): 3–4. http://dx.doi.org/10.1016/j.bpj.2019.06.014.

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3

Wei, Jiachen, and Fan Song. "Association equilibria for proteins interacted with crowders of short-range attraction in crowded environment." International Journal of Modern Physics B 31, no. 03 (2017): 1750007. http://dx.doi.org/10.1142/s0217979217500072.

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Based on a very simple coarse-grained colloidal model, here we implement an effective hard-sphere theory and numerical simulation to capture the general features of the association equilibria for globular proteins in crowded environment. We measure the activity coefficient, i.e., the deviation from ideal behavior of protein solution, and the crowding factor, i.e., the contribution of crowders to the association equilibria, for proteins in macromolecular crowding. The results show that the association balance in macromolecular crowding depends sensitively on the magnitude of protein–crowder att

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4

Snead, Wilton T., Carl C. Hayden, Avinash K. Gadok, et al. "Membrane fission by protein crowding." Proceedings of the National Academy of Sciences 114, no. 16 (2017): E3258—E3267. http://dx.doi.org/10.1073/pnas.1616199114.

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Membrane fission, which facilitates compartmentalization of biological processes into discrete, membrane-bound volumes, is essential for cellular life. Proteins with specific structural features including constricting rings, helical scaffolds, and hydrophobic membrane insertions are thought to be the primary drivers of fission. In contrast, here we report a mechanism of fission that is independent of protein structure—steric pressure among membrane-bound proteins. In particular, random collisions among crowded proteins generate substantial pressure, which if unbalanced on the opposite membrane

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5

Zosel, Franziska, Andrea Soranno, Karin J. Buholzer, Daniel Nettels, and Benjamin Schuler. "Depletion interactions modulate the binding between disordered proteins in crowded environments." Proceedings of the National Academy of Sciences 117, no. 24 (2020): 13480–89. http://dx.doi.org/10.1073/pnas.1921617117.

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Intrinsically disordered proteins (IDPs) abound in cellular regulation. Their interactions are often transitory and highly sensitive to salt concentration and posttranslational modifications. However, little is known about the effect of macromolecular crowding on the interactions of IDPs with their cellular targets. Here, we investigate the influence of crowding on the interaction between two IDPs that fold upon binding, with polyethylene glycol as a crowding agent. Single-molecule spectroscopy allows us to quantify the effects of crowding on a comprehensive set of observables simultaneously:

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6

Horton, Margaret R., Felix Höfling, Joachim O. Rädler, and Thomas Franosch. "Development of anomalous diffusion among crowding proteins." Soft Matter 6, no. 12 (2010): 2648. http://dx.doi.org/10.1039/b924149c.

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7

Dias, Rita S. "Role of Protein Self-Association on DNA Condensation and Nucleoid Stability in a Bacterial Cell Model." Polymers 11, no. 7 (2019): 1102. http://dx.doi.org/10.3390/polym11071102.

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Bacterial cells do not have a nuclear membrane that encompasses and isolates the genetic material. In addition, they do not possess histone proteins, which are responsible for the first levels of genome condensation in eukaryotes. Instead, there is a number of more or less specific nucleoid-associated proteins that induce DNA bridging, wrapping and bending. Many of these proteins self-assemble into oligomers. The crowded environment of cells is also believed to contribute to DNA condensation due to excluded volume effects. Ribosomes are protein-RNA complexes found in large concentrations in th

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8

Mukherji, Sutapa. "Run-length distribution of self-assembling cargos in crowded environments." Journal of Statistical Mechanics: Theory and Experiment 2025, no. 2 (2025): 023205. https://doi.org/10.1088/1742-5468/adab6f.

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Abstract Intracellular transport, carried out by motor proteins, is crucial for numerous biological functions of the cell. Cytoskeletal motor proteins such as kinesins and dyneins move on the biopolymer, microtubule, carrying different kinds of biomolecules as cargo to deliver these at required destinations. Such transport is often impeded by a crowded environment along the microtubule due to other motor proteins and various cellular organelles. Here, we study the motion of a self-assembling cargo that, during its translocation, can associate kinesins bound to the microtubules. This strategy i

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9

Banks, Daniel S., and Cécile Fradin. "Anomalous Diffusion of Proteins Due to Molecular Crowding." Biophysical Journal 89, no. 5 (2005): 2960–71. http://dx.doi.org/10.1529/biophysj.104.051078.

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10

Makowski, Lee, Diane J. Rodi, Suneeta Mandava, David D. L. Minh, David B. Gore, and Robert F. Fischetti. "Molecular Crowding Inhibits Intramolecular Breathing Motions in Proteins." Journal of Molecular Biology 375, no. 2 (2008): 529–46. http://dx.doi.org/10.1016/j.jmb.2007.07.075.

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11

Candotti, Michela, and Modesto Orozco. "The Differential Response of Proteins to Macromolecular Crowding." PLOS Computational Biology 12, no. 7 (2016): e1005040. http://dx.doi.org/10.1371/journal.pcbi.1005040.

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12

Perham, Michael, Loren Stagg, and Pernilla Wittung-Stafshede. "Macromolecular crowding increases structural content of folded proteins." FEBS Letters 581, no. 26 (2007): 5065–69. http://dx.doi.org/10.1016/j.febslet.2007.09.049.

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13

Chebotareva, Natalia A., Svetlana G. Roman, Vera A. Borzova, Tatiana B. Eronina, Valeriya V. Mikhaylova, and Boris I. Kurganov. "Chaperone-Like Activity of HSPB5: The Effects of Quaternary Structure Dynamics and Crowding." International Journal of Molecular Sciences 21, no. 14 (2020): 4940. http://dx.doi.org/10.3390/ijms21144940.

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Small heat-shock proteins (sHSPs) are ATP-independent molecular chaperones that interact with partially unfolded proteins, preventing their aberrant aggregation, thereby exhibiting a chaperone-like activity. Dynamics of the quaternary structure plays an important role in the chaperone-like activity of sHSPs. However, relationship between the dynamic structure of sHSPs and their chaperone-like activity remains insufficiently characterized. Many factors (temperature, ions, a target protein, crowding etc.) affect the structure and activity of sHSPs. The least studied is an effect of crowding on s

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14

Borzova, Vera A., Svetlana G. Roman, Anastasiya V. Pivovarova, and Natalia A. Chebotareva. "Effects of Molecular Crowding and Betaine on HSPB5 Interactions, with Target Proteins Differing in the Quaternary Structure and Aggregation Mechanism." International Journal of Molecular Sciences 23, no. 23 (2022): 15392. http://dx.doi.org/10.3390/ijms232315392.

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The aggregation of intracellular proteins may be enhanced under stress. The expression of heat-shock proteins (HSPs) and the accumulation of osmolytes are among the cellular protective mechanisms in these conditions. In addition, one should remember that the cell environment is highly crowded. The antiaggregation activity of HSPB5 and the effect on it of either a crowding agent (polyethylene glycol (PEG)) or an osmolyte (betaine), or their mixture, were tested on the aggregation of two target proteins that differ in the order of aggregation with respect to the protein: thermal aggregation of g

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15

Scott, Shane, Cynthia Shaheen, Brendon McGuinness, et al. "Single-molecule visualization of the effects of ionic strength and crowding on structure-mediated interactions in supercoiled DNA molecules." Nucleic Acids Research 47, no. 12 (2019): 6360–68. http://dx.doi.org/10.1093/nar/gkz408.

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Abstract DNA unwinding is an important cellular process involved in DNA replication, transcription and repair. In cells, molecular crowding caused by the presence of organelles, proteins, and other molecules affects numerous internal cellular structures. Here, we visualize plasmid DNA unwinding and binding dynamics to an oligonucleotide probe as functions of ionic strength, crowding agent concentration, and crowding agent species using single-molecule CLiC microscopy. We demonstrate increased probe–plasmid interaction over time with increasing concentration of 8 kDa polyethylene glycol (PEG),

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16

Demosthene, Bryan, Myeongsang Lee, Ryan R. Marracino, James B. Heidings, and Ellen Hyeran Kang. "Molecular Basis for Actin Polymerization Kinetics Modulated by Solution Crowding." Biomolecules 13, no. 5 (2023): 786. http://dx.doi.org/10.3390/biom13050786.

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Actin polymerization drives cell movement and provides cells with structural integrity. Intracellular environments contain high concentrations of solutes, including organic compounds, macromolecules, and proteins. Macromolecular crowding has been shown to affect actin filament stability and bulk polymerization kinetics. However, the molecular mechanisms behind how crowding influences individual actin filament assembly are not well understood. In this study, we investigated how crowding modulates filament assembly kinetics using total internal reflection fluorescence (TIRF) microscopy imaging a

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17

Gorensek-Benitez, Annelise H., Bryan Kirk, and Jeffrey K. Myers. "Protein Fibrillation under Crowded Conditions." Biomolecules 12, no. 7 (2022): 950. http://dx.doi.org/10.3390/biom12070950.

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Protein amyloid fibrils have widespread implications for human health. Over the last twenty years, fibrillation has been studied using a variety of crowding agents to mimic the packed interior of cells or to probe the mechanisms and pathways of the process. We tabulate and review these results by considering three classes of crowding agent: synthetic polymers, osmolytes and other small molecules, and globular proteins. While some patterns are observable for certain crowding agents, the results are highly variable and often depend on the specific pairing of crowder and fibrillating protein.

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18

André, Alain A. M., and Evan Spruijt. "Liquid–Liquid Phase Separation in Crowded Environments." International Journal of Molecular Sciences 21, no. 16 (2020): 5908. http://dx.doi.org/10.3390/ijms21165908.

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Biomolecular condensates play a key role in organizing cellular fluids such as the cytoplasm and nucleoplasm. Most of these non-membranous organelles show liquid-like properties both in cells and when studied in vitro through liquid–liquid phase separation (LLPS) of purified proteins. In general, LLPS of proteins is known to be sensitive to variations in pH, temperature and ionic strength, but the role of crowding remains underappreciated. Several decades of research have shown that macromolecular crowding can have profound effects on protein interactions, folding and aggregation, and it must,

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19

Al-Ayoubi, S. R., P. H. Schummel, M. Golub, J. Peters, and R. Winter. "Influence of cosolvents, self-crowding, temperature and pressure on the sub-nanosecond dynamics and folding stability of lysozyme." Physical Chemistry Chemical Physics 19, no. 22 (2017): 14230–37. http://dx.doi.org/10.1039/c7cp00705a.

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20

Ross, Murial L., Jeffrey Kunkel, Steven Long, and Prashanth Asuri. "Combined Effects of Confinement and Macromolecular Crowding on Protein Stability." International Journal of Molecular Sciences 21, no. 22 (2020): 8516. http://dx.doi.org/10.3390/ijms21228516.

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Confinement and crowding have been shown to affect protein fates, including folding, functional stability, and their interactions with self and other proteins. Using both theoretical and experimental studies, researchers have established the independent effects of confinement or crowding, but only a few studies have explored their effects in combination; therefore, their combined impact on protein fates is still relatively unknown. Here, we investigated the combined effects of confinement and crowding on protein stability using the pores of agarose hydrogels as a confining agent and the biopol

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21

Snead, Wilton T., Wade F. Zeno, Grace Kago, et al. "BAR scaffolds drive membrane fission by crowding disordered domains." Journal of Cell Biology 218, no. 2 (2018): 664–82. http://dx.doi.org/10.1083/jcb.201807119.

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Cellular membranes are continuously remodeled. The crescent-shaped bin-amphiphysin-rvs (BAR) domains remodel membranes in multiple cellular pathways. Based on studies of isolated BAR domains in vitro, the current paradigm is that BAR domain–containing proteins polymerize into cylindrical scaffolds that stabilize lipid tubules. But in nature, proteins that contain BAR domains often also contain large intrinsically disordered regions. Using in vitro and live cell assays, here we show that full-length BAR domain–containing proteins, rather than stabilizing membrane tubules, are instead surprising

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22

Li, Chao, Xiangxiang Zhang, Mingdong Dong, and Xiaojun Han. "Progress on Crowding Effect in Cell-like Structures." Membranes 12, no. 6 (2022): 593. http://dx.doi.org/10.3390/membranes12060593.

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Several biological macromolecules, such as proteins, nucleic acids, and polysaccharides, occupy about 30% of the space in cells, resulting in a crowded macromolecule environment. The crowding effect within cells exerts an impact on the functions of biological components, the assembly behavior of biomacromolecules, and the thermodynamics and kinetics of metabolic reactions. Cell-like structures provide confined and independent compartments for studying the working mechanisms of cells, which can be used to study the physiological functions arising from the crowding effect of macromolecules in ce

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23

Kim, Youngchan, and Jeetain Mittal. "Crowding Induced Coil-Globule Transitions of Intrinsically Disordered Proteins." Biophysical Journal 112, no. 3 (2017): 511a. http://dx.doi.org/10.1016/j.bpj.2016.11.2764.

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24

Qu, Youxing, and D. W. Bolen. "Efficacy of macromolecular crowding in forcing proteins to fold." Biophysical Chemistry 101-102 (December 2002): 155–65. http://dx.doi.org/10.1016/s0301-4622(02)00148-5.

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25

Mondal, Somnath, Ravula Thirupathi, and Hanudatta S. Atreya. "Carbon quantum dots as a macromolecular crowder." RSC Advances 5, no. 6 (2015): 4489–92. http://dx.doi.org/10.1039/c4ra14019b.

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26

Tokuriki, N., T. Yomo, Y. Katakura, K. Ogasawara, K. Yutani, and I. Urabe. "Crowding effect of proteins with random sequence in polyethylene glycol." Seibutsu Butsuri 40, supplement (2000): S172. http://dx.doi.org/10.2142/biophys.40.s172_2.

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27

Dey, Pinki, and Arnab Bhattacherjee. "Disparity in anomalous diffusion of proteins searching for their target DNA sites in a crowded medium is controlled by the size, shape and mobility of macromolecular crowders." Soft Matter 15, no. 9 (2019): 1960–69. http://dx.doi.org/10.1039/c8sm01933a.

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28

BESSA RAMOS, ESIO, KATHELIJNE WINTRAECKEN, ANS GEERLING, and RENKO DE VRIES. "SYNERGY OF DNA-BENDING NUCLEOID PROTEINS AND MACROMOLECULAR CROWDING IN CONDENSING DNA." Biophysical Reviews and Letters 02, no. 03n04 (2007): 259–65. http://dx.doi.org/10.1142/s1793048007000556.

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Many prokaryotic nucleoid proteins bend DNA and form extended helical protein-DNA fibers rather than condensed structures. On the other hand, it is known that such proteins (such as bacterial HU) strongly promote DNA condensation by macromolecular crowding. Using theoretical arguments, we show that this synergy is a simple consequence of the larger diameter and lower net charge density of the protein-DNA filaments as compared to naked DNA, and hence, should be quite general. To illustrate this generality, we use light-scattering to show that the 7kDa basic archaeal nucleoid protein Sso7d from

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29

TAKAGI, Fumiko, and Syoji TAKADA. "Structure formation of proteins and "Molecular crowding" : Molecular dynamics simulation." Seibutsu Butsuri 41, supplement (2001): S175. http://dx.doi.org/10.2142/biophys.41.s175_4.

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30

Simoncik, Oliver, Vlastimil Tichy, Michal Durech, et al. "Direct activation of HSF1 by macromolecular crowding and misfolded proteins." PLOS ONE 19, no. 11 (2024): e0312524. http://dx.doi.org/10.1371/journal.pone.0312524.

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Stress responses play a vital role in cellular survival against environmental challenges, often exploited by cancer cells to proliferate, counteract genomic instability, and resist therapeutic stress. Heat shock factor protein 1 (HSF1), a central transcription factor in stress response pathways, exhibits markedly elevated activity in cancer. Despite extensive research into the transcriptional role of HSF1, the mechanisms underlying its activation remain elusive. Upon exposure to conditions that induce protein damage, monomeric HSF1 undergoes rapid conformational changes and assembles into trim

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31

Wojciechowski, M., and Marek Cieplak. "Effects of confinement and crowding on folding of model proteins." Biosystems 94, no. 3 (2008): 248–52. http://dx.doi.org/10.1016/j.biosystems.2008.06.016.

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32

Arora, Simran, and Sri Rama Koti Ainavarapu. "Crowding-induced effects on the stability of ubiquitin-family proteins." Biophysical Journal 123, no. 3 (2024): 193a—194a. http://dx.doi.org/10.1016/j.bpj.2023.11.1242.

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33

Sulmann, Stefan, Daniele Dell'Orco, Valerio Marino, Petra Behnen, and Karl-Wilhelm Koch. "Conformational Changes in Calcium-Sensor Proteins under Molecular Crowding Conditions." Chemistry - A European Journal 20, no. 22 (2014): 6756–62. http://dx.doi.org/10.1002/chem.201402146.

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34

Šimončík, Oliver, Vlastimil Tichý, Michal Ďurech, et al. "Direct activation of HSF1 by macromolecular crowding and misfolded proteins." PLos ONE 19, no. 11 (2024): e0312524. https://doi.org/10.1371/journal.pone.0312524.

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Stress responses play a vital role in cellular survival against environmental challenges, often exploited by cancer cells to proliferate, counteract genomic instability, and resist therapeutic stress. Heat shock factor protein 1 (HSF1), a central transcription factor in stress response pathways, exhibits markedly elevated activity in cancer. Despite extensive research into the transcriptional role of HSF1, the mechanisms underlying its activation remain elusive. Upon exposure to conditions that induce protein damage, monomeric HSF1 undergoes rapid conformational changes and assembles into trim

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35

Byun, Wan Gi, Jihye Lee, Seungtaek Kim, and Seung Bum Park. "Harnessing stress granule formation by small molecules to inhibit the cellular replication of SARS-CoV-2." Chemical Communications 57, no. 93 (2021): 12476–79. http://dx.doi.org/10.1039/d1cc05508a.

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Small-molecule enhancers of cellular stress granules were identified by observing molecular crowding of proteins and RNAs in a time-dependent manner. Hit molecules inhibited the replication of SARS-CoV-2 by inducing stress granule formation.

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36

Shahid, Sumra, Ikramul Hasan, Faizan Ahmad, Md Imtaiyaz Hassan, and Asimul Islam. "Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder." Biomolecules 9, no. 9 (2019): 477. http://dx.doi.org/10.3390/biom9090477.

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There are a large number of biomolecules that are accountable for the extremely crowded intracellular environment, which is totally different from the dilute solutions, i.e., the idealized conditions. Such crowded environment due to the presence of macromolecules of different sizes, shapes, and composition governs the level of crowding inside a cell. Thus, we investigated the effect of different sizes and shapes of crowders (ficoll 70, dextran 70, and dextran 40), which are polysaccharide in nature, on the thermodynamic stability, structure, and functional activity of two model proteins using

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37

Qin, Sanbo, and Huan-Xiang Zhou. "Effects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins." Journal of Physical Chemistry Letters 4, no. 20 (2013): 3429–34. http://dx.doi.org/10.1021/jz401817x.

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38

Cino, Elio A., Mikko Karttunen, and Wing-Yiu Choy. "Effects of Molecular Crowding on the Dynamics of Intrinsically Disordered Proteins." PLoS ONE 7, no. 11 (2012): e49876. http://dx.doi.org/10.1371/journal.pone.0049876.

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39

Wei, Yuzhang, Isabel Mayoral-Delgado, Nicolas A. Stewart, and Marcus K. Dymond. "Macromolecular crowding and membrane binding proteins: The case of phospholipase A1." Chemistry and Physics of Lipids 218 (January 2019): 91–102. http://dx.doi.org/10.1016/j.chemphyslip.2018.12.006.

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40

Lemetti, Laura, Sami-Pekka Hirvonen, Dmitrii Fedorov, et al. "Molecular crowding facilitates assembly of spidroin-like proteins through phase separation." European Polymer Journal 112 (March 2019): 539–46. http://dx.doi.org/10.1016/j.eurpolymj.2018.10.010.

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41

de Vries, Renko. "DNA condensation in bacteria: Interplay between macromolecular crowding and nucleoid proteins." Biochimie 92, no. 12 (2010): 1715–21. http://dx.doi.org/10.1016/j.biochi.2010.06.024.

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42

Gupta, Munishwar Nath, and Vladimir N. Uversky. "Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins." International Journal of Molecular Sciences 24, no. 3 (2023): 2424. http://dx.doi.org/10.3390/ijms24032424.

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Transitions between the unfolded and native states of the ordered globular proteins are accompanied by the accumulation of several intermediates, such as pre-molten globules, wet molten globules, and dry molten globules. Structurally equivalent conformations can serve as native functional states of intrinsically disordered proteins. This overview captures the characteristics and importance of these molten globules in both structured and intrinsically disordered proteins. It also discusses examples of engineered molten globules. The formation of these intermediates under conditions of macromole

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43

Ishimori, Koichiro. "Regulatory Mechanisms of Electron Transfer from Cytochrome C to Cytochrome C Oxidase Under Simulated Intracellular Conditions." ECS Meeting Abstracts MA2025-01, no. 17 (2025): 1244. https://doi.org/10.1149/ma2025-01171244mtgabs.

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Electron transfer (ET) reactions are crucial for energy and substance metabolism in living organisms. Notably, ET reactions between proteins are believed to have protein-specific regulatory mechanisms distinct from those of small molecules, primarily due to the extended ET distance between redox centers within the fluctuating structures of proteins. The mitochondrial respiratory chain, comprising a series of interprotein ET reactions, functions to pump protons from the matrix to the intermembrane space by transferring electrons between proteins constituting the respiratory chain. This process

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44

Garner, M. M., and M. B. Burg. "Macromolecular crowding and confinement in cells exposed to hypertonicity." American Journal of Physiology-Cell Physiology 266, no. 4 (1994): C877—C892. http://dx.doi.org/10.1152/ajpcell.1994.266.4.c877.

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The nonideal properties of solutions containing high concentrations of macromolecules can result in enormous increases in the activity of the individual macromolecules. It has been proposed that molecular crowding and confinement occur in cells and are major determinants of the activity of the proteins and other intracellular macromolecules. This concept has important implications for cell volume regulation because, under crowded conditions, relatively small changes in concentration, consequent to alterations of water content, lead to large changes in macromolecular activity. This review consi

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45

Yang, Yin, Shen-Na Chen, Feng Yang, et al. "In-cell destabilization of a homodimeric protein complex detected by DEER spectroscopy." Proceedings of the National Academy of Sciences 117, no. 34 (2020): 20566–75. http://dx.doi.org/10.1073/pnas.2005779117.

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The complexity of the cellular medium can affect proteins’ properties, and, therefore, in-cell characterization of proteins is essential. We explored the stability and conformation of the first baculoviral IAP repeat (BIR) domain of X chromosome-linked inhibitor of apoptosis (XIAP), BIR1, as a model for a homodimer protein in human HeLa cells. We employed double electron–electron resonance (DEER) spectroscopy and labeling with redox stable and rigid Gd3+spin labels at three representative protein residues, C12 (flexible region), E22C, and N28C (part of helical residues 26 to 31) in the N-termi

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46

Höfig, Henning, Michele Cerminara, Ilona Ritter, et al. "Single-Molecule Studies on a FRET Biosensor: Lessons from a Comparison of Fluorescent Protein Equipped versus Dye-Labeled Species." Molecules 23, no. 12 (2018): 3105. http://dx.doi.org/10.3390/molecules23123105.

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Bacterial periplasmic binding proteins (PBPs) undergo a pronounced ligand-induced conformational change which can be employed to monitor ligand concentrations. The most common strategy to take advantage of this conformational change for a biosensor design is to use a Förster resonance energy transfer (FRET) signal. This can be achieved by attaching either two fluorescent proteins (FPs) or two organic fluorescent dyes of different colors to the PBPs in order to obtain an optical readout signal which is closely related to the ligand concentration. In this study we compare a FP-equipped and a dye

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47

Bokvist, Marcus, and Gerhard Gröbner. "Misfolding of Amyloidogenic Proteins at Membrane Surfaces: The Impact of Macromolecular Crowding." Journal of the American Chemical Society 129, no. 48 (2007): 14848–49. http://dx.doi.org/10.1021/ja076059o.

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48

Cheung, M. S., D. Klimov, and D. Thirumalai. "Molecular crowding enhances native state stability and refolding rates of globular proteins." Proceedings of the National Academy of Sciences 102, no. 13 (2005): 4753–58. http://dx.doi.org/10.1073/pnas.0409630102.

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49

Houser, Justin R., David J. Busch, David R. Bell, Brian Li, Pengyu Ren, and Jeanne C. Stachowiak. "The impact of physiological crowding on the diffusivity of membrane bound proteins." Soft Matter 12, no. 7 (2016): 2127–34. http://dx.doi.org/10.1039/c5sm02572a.

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50

Roman, Marisa I., Guoliang Yang, and Frank Ferrone. "Non Linear Effects of Macromolecular Crowding on the Mechanical Unfolding of Proteins." Biophysical Journal 104, no. 2 (2013): 566a. http://dx.doi.org/10.1016/j.bpj.2012.11.3138.

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