자료유형  

 학위논문

Control Number  

0016931967

International Standard Book Number  

9798379651039

Dewey Decimal Classification Number  

632

Main Entry-Personal Name  

Goncalves, Kevin Olegario.

Publication, Distribution, etc. (Imprint  

[S.l.] : Stanford University., 2022

Publication, Distribution, etc. (Imprint  

Ann Arbor : ProQuest Dissertations & Theses, 2022

Physical Description  

1 online resource(108 p.)

General Note  

Source: Dissertations Abstracts International, Volume: 84-12, Section: B.

General Note  

Advisor: Puglisi, Joseph D.;Wakatsuki, Soichi;Frydman, Judith.

Dissertation Note  

Thesis (Ph.D.)--Stanford University, 2022.

Restrictions on Access Note  

This item must not be sold to any third party vendors.

Summary, Etc.  

요약Protein function is dependent upon adoption of a native 3-D configuration whilst avoiding toxic conformations. Some proteins can fold spontaneously; however, the complexity of the proteome requires cellular cofactors called chaperones to ensure problematic proteins are natively folded. Chaperonins are a class of molecular chaperones that are universally conserved in all domains of life and contribute to the cellular proteostasis toolkit. They are 1-MDa complexes composed of two rings that undergo a dramatic conformational change with ATP hydrolysis to form an inner folding cavity. Chaperonins have significantly diverged in architecture, topology, and client repertoire so they are divided into two classes: group I and group II chaperonins. Group I chaperonins exist in prokarya whilst group II chaperonins are found in eukarya and archaea. All chaperonins help to orchestrate ATP-dependent client protein sequestration and refolding through encapsulation in the central folding cavity.This thesis is centered on enumerating the mechanism of a group II chaperonin found in M. Maripaludis (MmCpn), an archaeal methanogen. Biochemical and biophysical interrogation of structural moieties, chiefly the c-termini, were found to contribute to ATP hydrolysis, substrate re-folding, and complex integrity. New structural elements such as interfacial methionine fingers and electrostatic contacts were observed to undergo novel conformations, yielding new candidates for studying group II chaperonins in general. Electrostatic disruption of the c-termini allowed for dissection of multimeric states, including the long elusive single-ring species which could serve as a useful tool for understanding chaperonin biogenesis and function.

Subject Added Entry-Topical Term  

Prokaryotes.

Subject Added Entry-Topical Term  

Mass spectrometry.

Subject Added Entry-Topical Term  

Homeostasis.

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Protein folding.

Subject Added Entry-Topical Term  

Biosynthesis.

Subject Added Entry-Topical Term  

Binding sites.

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Scientific imaging.

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Biology.

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E coli.

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Catalysis.

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Heat shock proteins.

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Polypeptides.

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Analytical chemistry.

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Biophysics.

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Chemistry.

Subject Added Entry-Topical Term  

Physiology.

Added Entry-Corporate Name  

Stanford University.

Host Item Entry  

Dissertations Abstracts International. 84-12B.

Host Item Entry  

Dissertation Abstract International

Electronic Location and Access  

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Control Number  

joongbu:640666