Bound Water at Protein-Protein Interfaces Partners, Roles and Hydrophobic Bubbles as a Conserved Motif 英文参考文献.docVIP

下载本文档

6
0
约8.38万字
约 16页
2017-05-11 发布于上海
举报
版权申诉

Bound Water at Protein-Protein Interfaces Partners, Roles and Hydrophobic Bubbles as a Conserved Motif 英文参考文献.doc

1、原创力文档（book118）网站文档一经付费（服务费），不意味着购买了该文档的版权，仅供个人/单位学习、研究之用，不得用于商业用途，未经授权，严禁复制、发行、汇编、翻译或者网络传播等，侵权必究。。
2、本站所有内容均由合作方或网友上传，本站不对文档的完整性、权威性及其观点立场正确性做任何保证或承诺！文档内容仅供研究参考，付费前请自行鉴别。如您付费，意味着您自己接受本站规则且自行承担风险，本站不退款、不进行额外附加服务；查看《如何避免下载的几个坑》。如果您已付费下载过本站文档，您可以点击这里二次下载。
3、如文档侵犯商业秘密、侵犯著作权、侵犯人身权等，请点击“版权申诉”（推荐），也可以打举报电话：400-050-0827(电话支持时间：9:00-18:30)。
4、该文档为VIP文档，如果想要下载，成为VIP会员后，下载免费。
5、成为VIP后，下载本文档将扣除1次下载权益。下载后，不支持退款、换文档。如有疑问请联系我们。
6、成为VIP后，您将拥有八大权益，权益包括：VIP文档下载权益、阅读免打扰、文档格式转换、高级专利检索、专属身份标志、高级客服、多端互通、版权登记。
7、VIP文档为合作方或网友上传，每下载1次，网站将根据用户上传文档的质量评分、类型等，对文档贡献者给予高额补贴、流量扶持。如果你也想贡献VIP文档。上传文档

Bound Water at Protein-Protein Interfaces Partners, Roles and Hydrophobic Bubbles as a Conserved Motif 英文参考文献

BoundWateratProtein-ProteinInterfaces:Partners, RolesandHydrophobicBubblesasaConservedMotif MostafaH.Ahmed1,3,FrancescaSpyrakis4,5,6,PietroCozzini4,6,ParijatK.Tripathi4,AndreaMozzarelli5,6, J.NeelScarsdale2,3,MartinA.Safo1,3,GlenE.Kellogg1,2,3 * 1DepartmentofMedicinalChemistry,VirginiaCommonwealthUniversity,Richmond,Virginia,UnitedStatesofAmerica,2CenterfortheStudyofBiologicalComplexity, VirginiaCommonwealthUniversity,Richmond,Virginia,UnitedStatesofAmerica,3InstituteforStructuralBiologyandDrugDiscovery,VirginiaCommonwealthUniversity, Richmond, Virginia,United StatesofAmerica, 4Department ofGeneral andInorganic Chemistry, University ofParma, Parma,Italy, 5Department ofBiochemistry and MolecularBiology,UniversityofParma,Parma,Italy,6InstituteofBiostructuresandBiosystems,Rome,Italy Abstract Background: There is a great interest in understanding and exploiting protein-protein associations as new routes for treatinghumandisease.However,theseassociationsaredifficulttostructurallycharacterizeormodelalthoughthenumber of X-ray structures for protein-protein complexes is expanding. One feature of these complexes that has received little attentionistheroleofwatermoleculesintheinterfacialregion. Methodology:Adatasetof4741watermoleculesabstractedfrom179high-resolution(#2.30A)? X-raycrystalstructuresof protein-proteincomplexeswasanalyzedwithasuiteofmodelingtoolsbasedontheHINTforcefieldandhydrogen-bonding geometry.AmetrictermedRelevancewasusedtoclassifythegeneralrolesofthewatermolecules. Results:Thewatermoleculeswerefoundtobeinvolvedin:a)(bridging)interactionswithbothproteins(21%),b)favorable interactions with only one protein (53%), and c) no interactions with either protein (26%). This trend is shown to be independent of the crystallographic resolution. Interactions with residue backbones are consistent for all classes and accountfor21.5%ofallinteractions.Interactionswithpolarresiduesaresignificantlymorecommonforthefirstgroupand interactionswithnon-polarresiduesdominat