The statistical characteristics of protein hydration shells: A computer simulation

Water molecules and the hydrogen-bond network are essential structural components of many biological macromolecular systems, such as nucleic acids, as well as fibrillar and globular proteins. The water density in the protein hydration shell is known to differ from that of bulk water. In this paper,...

Full description

Saved in:
Bibliographic Details
Published in:Moscow University physics bulletin 2015-09, Vol.70 (5), p.362-367
Main Authors: Rubtcova, E. V., Solovey, A. B., Lobyshev, V. I.
Format: Article
Language:English
Subjects:
Mathematical and Computational Physics
Physics
Physics and Astronomy
Theoretical
Theoretical and Mathematical Physics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c288t-68a459578b15fcad90ecd7759a6b250c9812690c62ef3ed3522745d4139816903
cites cdi_FETCH-LOGICAL-c288t-68a459578b15fcad90ecd7759a6b250c9812690c62ef3ed3522745d4139816903
container_end_page 367
container_issue 5
container_start_page 362
container_title Moscow University physics bulletin
container_volume 70
creator Rubtcova, E. V.
Solovey, A. B.
Lobyshev, V. I.
description Water molecules and the hydrogen-bond network are essential structural components of many biological macromolecular systems, such as nucleic acids, as well as fibrillar and globular proteins. The water density in the protein hydration shell is known to differ from that of bulk water. In this paper, spatial density as function of the distance from the protein surface is discussed. The electric potential function is considered in the same way. The resulting profiles of the bound water density are characterized by the presence of several distinct maxima due to the existence of the regular structure of bound water at distances over 7 Å. The minor discrepancies that are observed in both radial functions for different proteins are explained by topological variations that were revealed earlier by studying the valence and dihedral angle-distribution functions for water bound to the same proteins.
doi_str_mv 10.3103/S0027134915050136
format article
fullrecord <record><control><sourceid>crossref_sprin</sourceid><recordid>TN_cdi_crossref_primary_10_3103_S0027134915050136</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>10_3103_S0027134915050136</sourcerecordid><originalsourceid>FETCH-LOGICAL-c288t-68a459578b15fcad90ecd7759a6b250c9812690c62ef3ed3522745d4139816903</originalsourceid><addsrcrecordid>eNp9kNFKwzAUhoMoWKcP4F1eoHqSNGni3RjqhIGg87pkaWo72qYk6cXe3mzzTvDqwPn-73D4Ebon8MAIsMdPAFoSVijCgQNh4gJlRLEil4WAS5QdcX7k1-gmhD0AF5SpDH1sW4tD1LELsTO6x6bVXpto_WkRsGvw5F203YjbQ-1T0I04tLbvwxNeYuOGaU5pHLph7k_0Fl01ug_27ncu0NfL83a1zjfvr2-r5SY3VMqYC6kLrngpd4Q3RtcKrKnLkistdpSDUZJQocAIahtma8YpLQteF4QlkgBbIHK-a7wLwdummnw3aH-oCFTHUqo_pSSHnp2QsuO39dXezX5Mb_4j_QDQB2PE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>The statistical characteristics of protein hydration shells: A computer simulation</title><source>Springer Nature</source><creator>Rubtcova, E. V. ; Solovey, A. B. ; Lobyshev, V. I.</creator><creatorcontrib>Rubtcova, E. V. ; Solovey, A. B. ; Lobyshev, V. I.</creatorcontrib><description>Water molecules and the hydrogen-bond network are essential structural components of many biological macromolecular systems, such as nucleic acids, as well as fibrillar and globular proteins. The water density in the protein hydration shell is known to differ from that of bulk water. In this paper, spatial density as function of the distance from the protein surface is discussed. The electric potential function is considered in the same way. The resulting profiles of the bound water density are characterized by the presence of several distinct maxima due to the existence of the regular structure of bound water at distances over 7 Å. The minor discrepancies that are observed in both radial functions for different proteins are explained by topological variations that were revealed earlier by studying the valence and dihedral angle-distribution functions for water bound to the same proteins.</description><identifier>ISSN: 0027-1349</identifier><identifier>EISSN: 1934-8460</identifier><identifier>DOI: 10.3103/S0027134915050136</identifier><language>eng</language><publisher>New York: Allerton Press</publisher><subject>Mathematical and Computational Physics ; Physics ; Physics and Astronomy ; Theoretical ; Theoretical and Mathematical Physics</subject><ispartof>Moscow University physics bulletin, 2015-09, Vol.70 (5), p.362-367</ispartof><rights>Allerton Press, Inc. 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c288t-68a459578b15fcad90ecd7759a6b250c9812690c62ef3ed3522745d4139816903</citedby><cites>FETCH-LOGICAL-c288t-68a459578b15fcad90ecd7759a6b250c9812690c62ef3ed3522745d4139816903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids></links><search><creatorcontrib>Rubtcova, E. V.</creatorcontrib><creatorcontrib>Solovey, A. B.</creatorcontrib><creatorcontrib>Lobyshev, V. I.</creatorcontrib><title>The statistical characteristics of protein hydration shells: A computer simulation</title><title>Moscow University physics bulletin</title><addtitle>Moscow Univ. Phys</addtitle><description>Water molecules and the hydrogen-bond network are essential structural components of many biological macromolecular systems, such as nucleic acids, as well as fibrillar and globular proteins. The water density in the protein hydration shell is known to differ from that of bulk water. In this paper, spatial density as function of the distance from the protein surface is discussed. The electric potential function is considered in the same way. The resulting profiles of the bound water density are characterized by the presence of several distinct maxima due to the existence of the regular structure of bound water at distances over 7 Å. The minor discrepancies that are observed in both radial functions for different proteins are explained by topological variations that were revealed earlier by studying the valence and dihedral angle-distribution functions for water bound to the same proteins.</description><subject>Mathematical and Computational Physics</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Theoretical</subject><subject>Theoretical and Mathematical Physics</subject><issn>0027-1349</issn><issn>1934-8460</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNp9kNFKwzAUhoMoWKcP4F1eoHqSNGni3RjqhIGg87pkaWo72qYk6cXe3mzzTvDqwPn-73D4Ebon8MAIsMdPAFoSVijCgQNh4gJlRLEil4WAS5QdcX7k1-gmhD0AF5SpDH1sW4tD1LELsTO6x6bVXpto_WkRsGvw5F203YjbQ-1T0I04tLbvwxNeYuOGaU5pHLph7k_0Fl01ug_27ncu0NfL83a1zjfvr2-r5SY3VMqYC6kLrngpd4Q3RtcKrKnLkistdpSDUZJQocAIahtma8YpLQteF4QlkgBbIHK-a7wLwdummnw3aH-oCFTHUqo_pSSHnp2QsuO39dXezX5Mb_4j_QDQB2PE</recordid><startdate>20150901</startdate><enddate>20150901</enddate><creator>Rubtcova, E. V.</creator><creator>Solovey, A. B.</creator><creator>Lobyshev, V. I.</creator><general>Allerton Press</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20150901</creationdate><title>The statistical characteristics of protein hydration shells: A computer simulation</title><author>Rubtcova, E. V. ; Solovey, A. B. ; Lobyshev, V. I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c288t-68a459578b15fcad90ecd7759a6b250c9812690c62ef3ed3522745d4139816903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Mathematical and Computational Physics</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Theoretical</topic><topic>Theoretical and Mathematical Physics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rubtcova, E. V.</creatorcontrib><creatorcontrib>Solovey, A. B.</creatorcontrib><creatorcontrib>Lobyshev, V. I.</creatorcontrib><collection>CrossRef</collection><jtitle>Moscow University physics bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rubtcova, E. V.</au><au>Solovey, A. B.</au><au>Lobyshev, V. I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The statistical characteristics of protein hydration shells: A computer simulation</atitle><jtitle>Moscow University physics bulletin</jtitle><stitle>Moscow Univ. Phys</stitle><date>2015-09-01</date><risdate>2015</risdate><volume>70</volume><issue>5</issue><spage>362</spage><epage>367</epage><pages>362-367</pages><issn>0027-1349</issn><eissn>1934-8460</eissn><abstract>Water molecules and the hydrogen-bond network are essential structural components of many biological macromolecular systems, such as nucleic acids, as well as fibrillar and globular proteins. The water density in the protein hydration shell is known to differ from that of bulk water. In this paper, spatial density as function of the distance from the protein surface is discussed. The electric potential function is considered in the same way. The resulting profiles of the bound water density are characterized by the presence of several distinct maxima due to the existence of the regular structure of bound water at distances over 7 Å. The minor discrepancies that are observed in both radial functions for different proteins are explained by topological variations that were revealed earlier by studying the valence and dihedral angle-distribution functions for water bound to the same proteins.</abstract><cop>New York</cop><pub>Allerton Press</pub><doi>10.3103/S0027134915050136</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0027-1349
ispartof Moscow University physics bulletin, 2015-09, Vol.70 (5), p.362-367
issn 0027-1349
1934-8460
language eng
recordid cdi_crossref_primary_10_3103_S0027134915050136
source Springer Nature
subjects Mathematical and Computational Physics
Physics
Physics and Astronomy
Theoretical
Theoretical and Mathematical Physics
title The statistical characteristics of protein hydration shells: A computer simulation
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T00%3A26%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-crossref_sprin&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20statistical%20characteristics%20of%20protein%20hydration%20shells:%20A%20computer%20simulation&rft.jtitle=Moscow%20University%20physics%20bulletin&rft.au=Rubtcova,%20E.%20V.&rft.date=2015-09-01&rft.volume=70&rft.issue=5&rft.spage=362&rft.epage=367&rft.pages=362-367&rft.issn=0027-1349&rft.eissn=1934-8460&rft_id=info:doi/10.3103/S0027134915050136&rft_dat=%3Ccrossref_sprin%3E10_3103_S0027134915050136%3C/crossref_sprin%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c288t-68a459578b15fcad90ecd7759a6b250c9812690c62ef3ed3522745d4139816903%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true