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Article ; Online: General mechanism of two-state protein folding kinetics.

Rollins, Geoffrey C / Dill, Ken A

Journal of the American Chemical Society

2014 Volume 136, Issue 32, Page(s) 11420–11427

Abstract: We describe here a general model of the kinetic mechanism of protein folding. In the Foldon Funnel Model, proteins fold in units of secondary structures, which form sequentially along the folding pathway, stabilized by tertiary interactions. The model ... ...

Abstract	We describe here a general model of the kinetic mechanism of protein folding. In the Foldon Funnel Model, proteins fold in units of secondary structures, which form sequentially along the folding pathway, stabilized by tertiary interactions. The model predicts that the free energy landscape has a volcano shape, rather than a simple funnel, that folding is two-state (single-exponential) when secondary structures are intrinsically unstable, and that each structure along the folding path is a transition state for the previous structure. It shows how sequential pathways are consistent with multiple stochastic routes on funnel landscapes, and it gives good agreement with the 9 order of magnitude dependence of folding rates on protein size for a set of 93 proteins, at the same time it is consistent with the near independence of folding equilibrium constant on size. This model gives estimates of folding rates of proteomes, leading to a median folding time in Escherichia coli of about 5 s.
MeSH term(s)	Anisotropy ; Biopolymers/chemistry ; Camphor/chemistry ; Deuterium Oxide/chemistry ; Graphite/chemistry ; Kinetics ; Magnetic Resonance Spectroscopy ; Molecular Weight ; Organic Chemicals ; Oxides/chemistry ; Proline/chemistry ; Protein Folding ; Proteins/chemistry ; Solutions ; Solvents/chemistry ; Sucrose/chemistry
Chemical Substances	Biopolymers ; Organic Chemicals ; Oxides ; Proteins ; Solutions ; Solvents ; Sucrose (57-50-1) ; Camphor (76-22-2) ; Graphite (7782-42-5) ; Proline (9DLQ4CIU6V) ; Deuterium Oxide (J65BV539M3)
Language	English
Publishing date	2014-07-30
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/ja5049434
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Article ; Online: Stochastic approach to the molecular counting problem in superresolution microscopy.

Rollins, Geoffrey C / Shin, Jae Yen / Bustamante, Carlos / Pressé, Steve

Proceedings of the National Academy of Sciences of the United States of America

2015 Volume 112, Issue 2, Page(s) E110–8

Abstract: Superresolution imaging methods--now widely used to characterize biological structures below the diffraction limit--are poised to reveal in quantitative detail the stoichiometry of protein complexes in living cells. In practice, the photophysical ... ...

Abstract	Superresolution imaging methods--now widely used to characterize biological structures below the diffraction limit--are poised to reveal in quantitative detail the stoichiometry of protein complexes in living cells. In practice, the photophysical properties of the fluorophores used as tags in superresolution methods have posed a severe theoretical challenge toward achieving this goal. Here we develop a stochastic approach to enumerate fluorophores in a diffraction-limited area measured by superresolution microscopy. The method is a generalization of aggregated Markov methods developed in the ion channel literature for studying gating dynamics. We show that the method accurately and precisely enumerates fluorophores in simulated data while simultaneously determining the kinetic rates that govern the stochastic photophysics of the fluorophores to improve the prediction's accuracy. This stochastic method overcomes several critical limitations of temporal thresholding methods.
MeSH term(s)	Fluorescent Dyes/chemistry ; Likelihood Functions ; Macromolecular Substances/chemistry ; Markov Chains ; Microscopy/methods ; Microscopy/statistics & numerical data ; Microscopy, Fluorescence/methods ; Microscopy, Fluorescence/statistics & numerical data ; Models, Chemical ; Molecular Imaging/methods ; Molecular Imaging/statistics & numerical data ; Multiprotein Complexes/chemistry ; Photochemical Processes ; Stochastic Processes
Chemical Substances	Fluorescent Dyes ; Macromolecular Substances ; Multiprotein Complexes
Language	English
Publishing date	2015-01-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1408071112
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Article: General Mechanism of Two-State Protein Folding Kinetics

Rollins, Geoffrey C / Dill Ken A

Journal of the American Chemical Society. 2014 Aug. 13, v. 136, no. 32

2014

Abstract	We describe here a general model of the kinetic mechanism of protein folding. In the Foldon Funnel Model, proteins fold in units of secondary structures, which form sequentially along the folding pathway, stabilized by tertiary interactions. The model predicts that the free energy landscape has a volcano shape, rather than a simple funnel, that folding is two-state (single-exponential) when secondary structures are intrinsically unstable, and that each structure along the folding path is a transition state for the previous structure. It shows how sequential pathways are consistent with multiple stochastic routes on funnel landscapes, and it gives good agreement with the 9 order of magnitude dependence of folding rates on protein size for a set of 93 proteins, at the same time it is consistent with the near independence of folding equilibrium constant on size. This model gives estimates of folding rates of proteomes, leading to a median folding time in Escherichia coli of about 5 s.
Keywords	Escherichia coli ; Gibbs free energy ; models ; protein folding ; proteins
Language	English
Dates of publication	2014-0813
Size	p. 11420-11427.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021%2Fja5049434
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Examinations of tRNA Range of Motion Using Simulations of Cryo-EM Microscopy and X-Ray Data.

Caulfield, Thomas R / Devkota, Batsal / Rollins, Geoffrey C

Journal of biophysics (Hindawi Publishing Corporation : Online)

2011 Volume 2011, Page(s) 219515

Abstract: We examined tRNA flexibility using a combination of steered and unbiased molecular dynamics simulations. Using Maxwell's demon algorithm, molecular dynamics was used to steer X-ray structure data toward that from an alternative state obtained from ... ...

Abstract	We examined tRNA flexibility using a combination of steered and unbiased molecular dynamics simulations. Using Maxwell's demon algorithm, molecular dynamics was used to steer X-ray structure data toward that from an alternative state obtained from cryogenic-electron microscopy density maps. Thus, we were able to fit X-ray structures of tRNA onto cryogenic-electron microscopy density maps for hybrid states of tRNA. Additionally, we employed both Maxwell's demon molecular dynamics simulations and unbiased simulation methods to identify possible ribosome-tRNA contact areas where the ribosome may discriminate tRNAs during translation. Herein, we collected >500 ns of simulation data to assess the global range of motion for tRNAs. Biased simulations can be used to steer between known conformational stop points, while unbiased simulations allow for a general testing of conformational space previously unexplored. The unbiased molecular dynamics data describes the global conformational changes of tRNA on a sub-microsecond time scale for comparison with steered data. Additionally, the unbiased molecular dynamics data was used to identify putative contacts between tRNA and the ribosome during the accommodation step of translation. We found that the primary contact regions were H71 and H92 of the 50S subunit and ribosomal proteins L14 and L16.
Language	English
Publishing date	2011-03-28
Publishing country	Egypt
Document type	Journal Article
ZDB-ID	2448923-2
ISSN	1687-8019 ; 1687-8000
ISSN (online)	1687-8019
ISSN	1687-8000
DOI	10.1155/2011/219515
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Article ; Online: Examinations of tRNA Range of Motion Using Simulations of Cryo-EM Microscopy and X-Ray Data

Thomas R. Caulfield / Batsal Devkota / Geoffrey C. Rollins

Journal of Biophysics, Vol

2011 Volume 2011

Abstract	We examined tRNA flexibility using a combination of steered and unbiased molecular dynamics simulations. Using Maxwell's demon algorithm, molecular dynamics was used to steer X-ray structure data toward that from an alternative state obtained from cryogenic-electron microscopy density maps. Thus, we were able to fit X-ray structures of tRNA onto cryogenic-electron microscopy density maps for hybrid states of tRNA. Additionally, we employed both Maxwell's demon molecular dynamics simulations and unbiased simulation methods to identify possible ribosome-tRNA contact areas where the ribosome may discriminate tRNAs during translation. Herein, we collected >500 ns of simulation data to assess the global range of motion for tRNAs. Biased simulations can be used to steer between known conformational stop points, while unbiased simulations allow for a general testing of conformational space previously unexplored. The unbiased molecular dynamics data describes the global conformational changes of tRNA on a sub-microsecond time scale for comparison with steered data. Additionally, the unbiased molecular dynamics data was used to identify putative contacts between tRNA and the ribosome during the accommodation step of translation. We found that the primary contact regions were H71 and H92 of the 50S subunit and ribosomal proteins L14 and L16.
Keywords	Biology (General) ; QH301-705.5
Subject code	541
Language	English
Publishing date	2011-01-01T00:00:00Z
Publisher	Hindawi Publishing Corporation
Document type	Article ; Online
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Article ; Online: The role of DNA twist in the packaging of viral genomes.

Rollins, Geoffrey C / Petrov, Anton S / Harvey, Stephen C

Biophysical journal

2008 Volume 94, Issue 5, Page(s) L38–40

Abstract: We performed molecular dynamics simulations of the genome packaging of bacteriophage P4 using two coarse-grained models of DNA. The first model, 1DNA6 (one pseudo-atom per six DNA basepairs), represents DNA as a string of beads, for which DNA torsions ... ...

Abstract	We performed molecular dynamics simulations of the genome packaging of bacteriophage P4 using two coarse-grained models of DNA. The first model, 1DNA6 (one pseudo-atom per six DNA basepairs), represents DNA as a string of beads, for which DNA torsions are undefined. The second model, 3DNA6 (three pseudo-atoms per six DNA basepairs), represents DNA as a series of base planes with torsions defined by the angles between successive planes. Bacteriophage P4 was packaged with 1DNA6, 3DNA6 in a torsionally relaxed state, and 3DNA6 in a torsionally strained state. We observed good agreement between the packed conformation of 1DNA6 and the packed conformations of 3DNA6. The free energies of packaging were in agreement, as well. Our results suggest that DNA torsions can be omitted from coarse-grained bacteriophage packaging simulations without significantly altering the DNA conformations or free energies of packaging that the simulations predict.
MeSH term(s)	Bacteriophages/genetics ; Bacteriophages/metabolism ; Base Pairing ; Computer Simulation ; DNA Packaging/genetics ; DNA Packaging/physiology ; DNA, Viral/chemistry ; DNA, Viral/genetics ; Genome, Viral/genetics ; Genome, Viral/physiology ; Nucleic Acid Conformation ; Virus Assembly/physiology
Chemical Substances	DNA, Viral
Language	English
Publishing date	2008-03-01
Publishing country	United States
Document type	Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1529/biophysj.107.126698
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Article: Institutional implementation of clinical tumor profiling on an unselected cancer population.

Sholl, Lynette M / Do, Khanh / Shivdasani, Priyanka / Cerami, Ethan / Dubuc, Adrian M / Kuo, Frank C / Garcia, Elizabeth P / Jia, Yonghui / Davineni, Phani / Abo, Ryan P / Pugh, Trevor J / van Hummelen, Paul / Thorner, Aaron R / Ducar, Matthew / Berger, Alice H / Nishino, Mizuki / Janeway, Katherine A / Church, Alanna / Harris, Marian /

JCI insight

2016 Volume 1, Issue 19, Page(s) e87062

Abstract: BACKGROUND. ...

Abstract	BACKGROUND.
MeSH term(s)	DNA Mutational Analysis ; Genomics ; High-Throughput Nucleotide Sequencing ; Humans ; Mutation ; Neoplasms/genetics ; Precision Medicine ; Retrospective Studies
Language	English
Publishing date	2016-11-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2379-3708
ISSN	2379-3708
DOI	10.1172/jci.insight.87062
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Article ; Online: Extreme Competence: Keystone Hosts of Infections.

Martin, Lynn B / Addison, BriAnne / Bean, Andrew G D / Buchanan, Katherine L / Crino, Ondi L / Eastwood, Justin R / Flies, Andrew S / Hamede, Rodrigo / Hill, Geoffrey E / Klaassen, Marcel / Koch, Rebecca E / Martens, Johanne M / Napolitano, Constanza / Narayan, Edward J / Peacock, Lee / Peel, Alison J / Peters, Anne / Raven, Nynke / Risely, Alice /

Roast, Michael J / Rollins, Lee A / Ruiz-Aravena, Manuel / Selechnik, Dan / Stokes, Helena S / Ujvari, Beata / Grogan, Laura F

Trends in ecology & evolution

2019 Volume 34, Issue 4, Page(s) 303–314

Abstract: Individual hosts differ extensively in their competence for parasites, but traditional research has discounted this variation, partly because modeling such heterogeneity is difficult. This discounting has diminished as tools have improved and recognition ...

Abstract	Individual hosts differ extensively in their competence for parasites, but traditional research has discounted this variation, partly because modeling such heterogeneity is difficult. This discounting has diminished as tools have improved and recognition has grown that some hosts, the extremely competent, can have exceptional impacts on disease dynamics. Most prominent among these hosts are the superspreaders, but other forms of extreme competence (EC) exist and others await discovery; each with potentially strong but distinct implications for disease emergence and spread. Here, we propose a framework for the study and discovery of EC, suitable for different host-parasite systems, which we hope enhances our understanding of how parasites circulate and evolve in host communities.
MeSH term(s)	Animals ; Host-Parasite Interactions ; Parasites
Keywords	covid19
Language	English
Publishing date	2019-01-29
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	284965-3
ISSN	1872-8383 ; 0169-5347
ISSN (online)	1872-8383
ISSN	0169-5347
DOI	10.1016/j.tree.2018.12.009
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Article ; Online: Not all quiet on the noise front.

McCullagh, Emma / Farlow, Justin / Fuller, Christopher / Girard, Juliet / Lipinski-Kruszka, Joanna / Lu, Dan / Noriega, Thomas / Rollins, Geoffrey / Spitzer, Russell / Todhunter, Michael / El-Samad, Hana

Nature chemical biology

2009 Volume 5, Issue 10, Page(s) 699–704

Abstract: Phenotypic diversity exists even within isogenic populations of cells. Such nongenetic individuality may have wide implications for our understanding of many biological processes. The field of study concerned with the investigation of nongenetic ... ...

Abstract	Phenotypic diversity exists even within isogenic populations of cells. Such nongenetic individuality may have wide implications for our understanding of many biological processes. The field of study concerned with the investigation of nongenetic individuality, also known as the 'biology of noise', is ripe with exciting scientific opportunities and challenges.
MeSH term(s)	Aging/genetics ; Aging/physiology ; Cell Communication ; Evolution, Molecular ; Gene Expression ; Phenotype ; Stochastic Processes
Language	English
Publishing date	2009-09-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2202962-X
ISSN	1552-4469 ; 1552-4450
ISSN (online)	1552-4469
ISSN	1552-4450
DOI	10.1038/nchembio.222
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Article ; Online: Search for Subsolar-Mass Binaries in the First Half of Advanced LIGO's and Advanced Virgo's Third Observing Run.

Abbott, R / Abbott, T D / Acernese, F / Ackley, K / Adams, C / Adhikari, N / Adhikari, R X / Adya, V B / Affeldt, C / Agarwal, D / Agathos, M / Agatsuma, K / Aggarwal, N / Aguiar, O D / Aiello, L / Ain, A / Ajith, P / Albanesi, S / Allocca, A /

Altin, P A / Amato, A / Anand, C / Anand, S / Ananyeva, A / Anderson, S B / Anderson, W G / Andrade, T / Andres, N / Andrić, T / Angelova, S V / Ansoldi, S / Antelis, J M / Antier, S / Appert, S / Arai, K / Araya, M C / Areeda, J S / Arène, M / Arnaud, N / Aronson, S M / Arun, K G / Asali, Y / Ashton, G / Assiduo, M / Aston, S M / Astone, P / Aubin, F / Austin, C / Babak, S / Badaracco, F / Bader, M K M / Badger, C / Bae, S / Baer, A M / Bagnasco, S / Bai, Y / Baird, J / Ball, M / Ballardin, G / Ballmer, S W / Balsamo, A / Baltus, G / Banagiri, S / Bankar, D / Barayoga, J C / Barbieri, C / Barish, B C / Barker, D / Barneo, P / Barone, F / Barr, B / Barsotti, L / Barsuglia, M / Barta, D / Bartlett, J / Barton, M A / Bartos, I / Bassiri, R / Basti, A / Bawaj, M / Bayley, J C / Baylor, A C / Bazzan, M / Bécsy, B / Bedakihale, V M / Bejger, M / Belahcene, I / Benedetto, V / Beniwal, D / Bennett, T F / Bentley, J D / BenYaala, M / Bergamin, F / Berger, B K / Bernuzzi, S / Berry, C P L / Bersanetti, D / Bertolini, A / Betzwieser, J / Beveridge, D / Bhandare, R / Bhardwaj, U / Bhattacharjee, D / Bhaumik, S / Bilenko, I A / Billingsley, G / Bini, S / Birney, R / Birnholtz, O / Biscans, S / Bischi, M / Biscoveanu, S / Bisht, A / Biswas, B / Bitossi, M / Bizouard, M-A / Blackburn, J K / Blair, C D / Blair, D G / Blair, R M / Bobba, F / Bode, N / Boer, M / Bogaert, G / Boldrini, M / Bonavena, L D / Bondu, F / Bonilla, E / Bonnand, R / Booker, P / Boom, B A / Bork, R / Boschi, V / Bose, N / Bose, S / Bossilkov, V / Boudart, V / Bouffanais, Y / Bozzi, A / Bradaschia, C / Brady, P R / Bramley, A / Branch, A / Branchesi, M / Brau, J E / Breschi, M / Briant, T / Briggs, J H / Brillet, A / Brinkmann, M / Brockill, P / Brooks, A F / Brooks, J / Brown, D D / Brunett, S / Bruno, G / Bruntz, R / Bryant, J / Bulik, T / Bulten, H J / Buonanno, A / Buscicchio, R / Buskulic, D / Buy, C / Byer, R L / Cadonati, L / Cagnoli, G / Cahillane, C / Bustillo, J Calderón / Callaghan, J D / Callister, T A / Calloni, E / Cameron, J / Camp, J B / Canepa, M / Canevarolo, S / Cannavacciuolo, M / Cannon, K C / Cao, H / Capote, E / Carapella, G / Carbognani, F / Carlin, J B / Carney, M F / Carpinelli, M / Carrillo, G / Carullo, G / Carver, T L / Diaz, J Casanueva / Casentini, C / Castaldi, G / Caudill, S / Cavaglià, M / Cavalier, F / Cavalieri, R / Ceasar, M / Cella, G / Cerdá-Durán, P / Cesarini, E / Chaibi, W / Chakravarti, K / Subrahmanya, S Chalathadka / Champion, E / Chan, C-H / Chan, C / Chan, C L / Chan, K / Chandra, K / Chanial, P / Chao, S / Charlton, P / Chase, E A / Chassande-Mottin, E / Chatterjee, C / Chatterjee, Debarati / Chatterjee, Deep / Chaturvedi, M / Chaty, S / Chatziioannou, K / Chen, H Y / Chen, J / Chen, X / Chen, Y / Chen, Z / Cheng, H / Cheong, C K / Cheung, H Y / Chia, H Y / Chiadini, F / Chiarini, G / Chierici, R / Chincarini, A / Chiofalo, M L / Chiummo, A / Cho, G / Cho, H S / Choudhary, R K / Choudhary, S / Christensen, N / Chu, Q / Chua, S / Chung, K W / Ciani, G / Ciecielag, P / Cieślar, M / Cifaldi, M / Ciobanu, A A / Ciolfi, R / Cipriano, F / Cirone, A / Clara, F / Clark, E N / Clark, J A / Clarke, L / Clearwater, P / Clesse, S / Cleva, F / Coccia, E / Codazzo, E / Cohadon, P-F / Cohen, D E / Cohen, L / Colleoni, M / Collette, C G / Colombo, A / Colpi, M / Compton, C M / Constancio, M / Conti, L / Cooper, S J / Corban, P / Corbitt, T R / Cordero-Carrión, I / Corezzi, S / Corley, K R / Cornish, N / Corre, D / Corsi, A / Cortese, S / Costa, C A / Cotesta, R / Coughlin, M W / Coulon, J-P / Countryman, S T / Cousins, B / Couvares, P / Coward, D M / Cowart, M J / Coyne, D C / Coyne, R / Creighton, J D E / Creighton, T D / Criswell, A W / Croquette, M / Crowder, S G / Cudell, J R / Cullen, T J / Cumming, A / Cummings, R / Cunningham, L / Cuoco, E / Curyło, M / Dabadie, P / Canton, T Dal / Dall'Osso, S / Dálya, G / Dana, A / DaneshgaranBajastani, L M / D'Angelo, B / Danilishin, S / D'Antonio, S / Danzmann, K / Darsow-Fromm, C / Dasgupta, A / Datrier, L E H / Datta, S / Dattilo, V / Dave, I / Davier, M / Davies, G S / Davis, D / Davis, M C / Daw, E J / Dean, R / DeBra, D / Deenadayalan, M / Degallaix, J / De Laurentis, M / Deléglise, S / Del Favero, V / De Lillo, F / De Lillo, N / Del Pozzo, W / DeMarchi, L M / De Matteis, F / D'Emilio, V / Demos, N / Dent, T / Depasse, A / De Pietri, R / De Rosa, R / De Rossi, C / DeSalvo, R / De Simone, R / Dhurandhar, S / Díaz, M C / Diaz-Ortiz, M / Didio, N A / Dietrich, T / Di Fiore, L / Di Fronzo, C / Di Giorgio, C / Di Giovanni, F / Di Giovanni, M / Di Girolamo, T / Di Lieto, A / Ding, B / Di Pace, S / Di Palma, I / Di Renzo, F / Divakarla, A K / Dmitriev, A / Doctor, Z / D'Onofrio, L / Donovan, F / Dooley, K L / Doravari, S / Dorrington, I / Drago, M / Driggers, J C / Drori, Y / Ducoin, J-G / Dupej, P / Durante, O / D'Urso, D / Duverne, P-A / Dwyer, S E / Eassa, C / Easter, P J / Ebersold, M / Eckhardt, T / Eddolls, G / Edelman, B / Edo, T B / Edy, O / Effler, A / Eichholz, J / Eikenberry, S S / Eisenmann, M / Eisenstein, R A / Ejlli, A / Engelby, E / Errico, L / Essick, R C / Estellés, H / Estevez, D / Etienne, Z / Etzel, T / Evans, M / Evans, T M / Ewing, B E / Fafone, V / Fair, H / Fairhurst, S / Farah, A M / Farinon, S / Farr, B / Farr, W M / Farrow, N W / Fauchon-Jones, E J / Favaro, G / Favata, M / Fays, M / Fazio, M / Feicht, J / Fejer, M M / Fekecs, B / Fenyvesi, E / Ferguson, D L / Fernandez-Galiana, A / Ferrante, I / Ferreira, T A / Fidecaro, F / Figura, P / Fiori, I / Fishbach, M / Fisher, R P / Fittipaldi, R / Fiumara, V / Flaminio, R / Floden, E / Fong, H / Font, J A / Fornal, B / Forsyth, P W F / Franke, A / Frasca, S / Frasconi, F / Frederick, C / Freed, J P / Frei, Z / Freise, A / Frey, R / Fritschel, P / Frolov, V V / Fronzé, G G / Fulda, P / Fyffe, M / Gabbard, H A / Gadre, B U / Gair, J R / Gais, J / Galaudage, S / Gamba, R / Ganapathy, D / Ganguly, A / Gaonkar, S G / Garaventa, B / García-Núñez, C / García-Quirós, C / Garufi, 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Physical review letters

2022 Volume 129, Issue 6, Page(s) 61104

Abstract: We report on a search for compact binary coalescences where at least one binary component has a mass between 0.2 M_{⊙} and 1.0 M_{⊙} in Advanced LIGO and Advanced Virgo data collected between 1 April 2019 1500 UTC and 1 October 2019 1500 UTC. We extend ...

Abstract	We report on a search for compact binary coalescences where at least one binary component has a mass between 0.2 M_{⊙} and 1.0 M_{⊙} in Advanced LIGO and Advanced Virgo data collected between 1 April 2019 1500 UTC and 1 October 2019 1500 UTC. We extend our previous analyses in two main ways: we include data from the Virgo detector and we allow for more unequal mass systems, with mass ratio q≥0.1. We do not report any gravitational-wave candidates. The most significant trigger has a false alarm rate of 0.14 yr^{-1}. This implies an upper limit on the merger rate of subsolar binaries in the range [220-24200] Gpc^{-3} yr^{-1}, depending on the chirp mass of the binary. We use this upper limit to derive astrophysical constraints on two phenomenological models that could produce subsolar-mass compact objects. One is an isotropic distribution of equal-mass primordial black holes. Using this model, we find that the fraction of dark matter in primordial black holes in the mass range 0.2 M_{⊙}<m_{PBH}<1.0 M_{⊙} is f_{PBH}≡Ω_{PBH}/Ω_{DM}≲6%. This improves existing constraints on primordial black hole abundance by a factor of ∼3. The other is a dissipative dark matter model, in which fermionic dark matter can collapse and form black holes. The upper limit on the fraction of dark matter black holes depends on the minimum mass of the black holes that can be formed: the most constraining result is obtained at M_{min}=1 M_{⊙}, where f_{DBH}≡Ω_{DBH}/Ω_{DM}≲0.003%. These are the first constraints placed on dissipative dark models by subsolar-mass analyses.<br />
Language	English
Publishing date	2022-08-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	208853-8
ISSN	1079-7114 ; 0031-9007
ISSN (online)	1079-7114
ISSN	0031-9007
DOI	10.1103/PhysRevLett.129.061104
Database	MEDical Literature Analysis and Retrieval System OnLINE

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