dc.identifier.uri | http://hdl.handle.net/11401/76642 | |
dc.description.sponsorship | This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree. | en_US |
dc.format | Monograph | |
dc.format.medium | Electronic Resource | en_US |
dc.language.iso | en_US | |
dc.publisher | The Graduate School, Stony Brook University: Stony Brook, NY. | |
dc.type | Dissertation | |
dcterms.abstract | This dissertation will cover three distinct topics of protein stability, non-equilibrium thermodynamics and scientometrics. In senescent organisms aging is correlated with oxidative damage of proteins. The damage done to proteins destabilizes them inhibiting their function. The implications of a simplified model based on side-chain modification of charged residues using Debye-H\"{u}ckel theory will be presented. Short length and highly charged proteins are susceptible to destabilization from oxidative damage. Among these proteins already studied in aging several proteins fit this description of being short and highly charged. There is a noticeable enrichment of short-highly-charged proteins in categories of proteins known to be important in aging. Maximum Caliber (MaxCal) is a potential theory of non-equilibrium statistical mechanics. It will be shown how MaxCal is used to derive the Onsager reciprocal relations, Green-Kubo relations and Prigogine’s Principle and extend these relations beyond the near-equilibrium regime. The last topic is the citation and publication trends of papers and authors, respectively. A discussion of how pure-birth processes can be applied to understanding citation trends and how birth-processes can be used in classifying papers into different categories of performance. | |
dcterms.abstract | This dissertation will cover three distinct topics of protein stability, non-equilibrium thermodynamics and scientometrics. In senescent organisms aging is correlated with oxidative damage of proteins. The damage done to proteins destabilizes them inhibiting their function. The implications of a simplified model based on side-chain modification of charged residues using Debye-H\"{u}ckel theory will be presented. Short length and highly charged proteins are susceptible to destabilization from oxidative damage. Among these proteins already studied in aging several proteins fit this description of being short and highly charged. There is a noticeable enrichment of short-highly-charged proteins in categories of proteins known to be important in aging. Maximum Caliber (MaxCal) is a potential theory of non-equilibrium statistical mechanics. It will be shown how MaxCal is used to derive the Onsager reciprocal relations, Green-Kubo relations and Prigogine’s Principle and extend these relations beyond the near-equilibrium regime. The last topic is the citation and publication trends of papers and authors, respectively. A discussion of how pure-birth processes can be applied to understanding citation trends and how birth-processes can be used in classifying papers into different categories of performance. | |
dcterms.available | 2017-09-20T16:50:51Z | |
dcterms.contributor | Fernandez-Serra, Marivi | en_US |
dcterms.contributor | Dill, Ken A | en_US |
dcterms.contributor | Metcalf, Harold J | en_US |
dcterms.contributor | Balazsi, Gabor. | en_US |
dcterms.creator | Hazoglou, Michael John | |
dcterms.dateAccepted | 2017-09-20T16:50:51Z | |
dcterms.dateSubmitted | 2017-09-20T16:50:51Z | |
dcterms.description | Department of Physics | en_US |
dcterms.extent | 90 pg. | en_US |
dcterms.format | Monograph | |
dcterms.format | Application/PDF | en_US |
dcterms.identifier | http://hdl.handle.net/11401/76642 | |
dcterms.issued | 2016-12-01 | |
dcterms.language | en_US | |
dcterms.provenance | Made available in DSpace on 2017-09-20T16:50:51Z (GMT). No. of bitstreams: 1
Hazoglou_grad.sunysb_0771E_13103.pdf: 4670612 bytes, checksum: 46296a79655dd1a78c374cb53fe2064f (MD5)
Previous issue date: 1 | en |
dcterms.publisher | The Graduate School, Stony Brook University: Stony Brook, NY. | |
dcterms.subject | Physics | |
dcterms.subject | bibliometrics, Entropy, non-equilibrium thermodynamics, Protein stability | |
dcterms.title | Topics in Statistical Physics: Protein Stability, Non-Equilibrium Thermodynamics, and | |
dcterms.type | Dissertation | |