Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry. - Wikidata - awgldk - TriplyDB

Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.

Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.

http://www.wikidata.org/entity/Q36835434

about

The nature of protein folding pathways GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding Protein Structural Analysis via Mass Spectrometry-Based Proteomics Propensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins.Type 1 and Type 2 scenarios in hydrogen exchange mass spectrometry studies on protein-ligand complexes.Hydrogen Exchange Mass Spectrometry.UniCon3D: de novo protein structure prediction using united-residue conformational search via stepwise, probabilistic sampling Defining a length scale for millisecond-timescale protein conformational exchange.Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?General mechanism of two-state protein folding kinetics.Clusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability.High-resolution epitope mapping by HX MS reveals the pathogenic mechanism and a possible therapy for autoimmune TTP syndrome.Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection.Fast protein folding kinetics Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule.Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Conformational States of macromolecular assemblies explored by integrative structure calculation.Autonomously folding protein fragments reveal differences in the energy landscapes of homologous RNases H Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.Interaction Networks in Protein Folding via Atomic-Resolution Experiments and Long-Time-Scale Molecular Dynamics Simulations Cytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway.Probing the protein-folding mechanism using denaturant and temperature effects on rate constants Revealing what gets buried first in protein folding.Energetic Coupling between Ligand Binding and Dimerization in Escherichia coli Phosphoglycerate Mutase Folding of a large protein at high structural resolution.Mutational landscape of antibody variable domains reveals a switch modulating the interdomain conformational dynamics and antigen binding.Fifty years of DNA "breathing": Reflections on old and new approaches.Higher order structure characterization of protein therapeutics by hydrogen/deuterium exchange mass spectrometry.Early Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity.Ultrafast hydrogen exchange reveals specific structural events during the initial stages of folding of cytochrome c Exploring the Sequence-based Prediction of Folding Initiation Sites in Proteins.Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution.How cooperative are protein folding and unfolding transitions?Global and Local Conformation of Human IgG Antibody Variants Rationalizes Loss of Thermodynamic Stability.High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.Unravelling the mysteries of sub-second biochemical processes using time-resolved mass spectrometry.Protein Folding-How and Why: By Hydrogen Exchange, Fragment Separation, and Mass Spectrometry Single-molecule chemo-mechanical unfolding reveals multiple transition state barriers in a small single-domain protein.Salt bridge as a gatekeeper against partial unfolding.

P2860

Q26998903-DCB16EF2-424A-4EBB-8955-F740AD07F622 Q27683698-E036BF19-EE92-4A59-A15B-DDE465587C64 Q28818005-27A729A5-2A6F-449F-AE2E-C31F6C8B4C07 Q30009420-3381DEBC-A7A2-4B4C-B468-F10A8015E4D5 Q30367857-6364EF9A-F445-441D-84D9-01F735FC2AFE Q30383686-FE03B368-C81F-4E98-B589-A6F27DF77260 Q30388897-84945080-7CD1-4D5D-AFC9-AF37A565F769 Q30651701-1D9F0736-F8EC-43E4-BE5C-DDAE1DD09B3F Q30691136-63BF4DDF-61F7-40F4-8861-CBF2C5724F3C Q30838291-C160C9CE-B95D-4731-8631-4C31F0FAB575 Q31031804-D3F932C4-6A08-4C88-BDCB-3069E72D4010 Q33424684-58CD96CE-D326-4D9E-A95A-43E51D6E4945 Q33689504-BFA1E10A-6720-4B89-ABF1-CA7BD08F8AA0 Q33719314-13F50660-B3CF-409E-AD10-FED44E31E271 Q34383815-D4B3843B-81FD-4A56-9CBD-683CFDA0B209 Q34543806-1AA14244-374B-4976-B5BC-61FDA14E984C Q34870033-1E07894A-1D48-4F63-B85C-6224F8454F2C Q34980210-D5FB426D-FF69-4C16-8B02-4B7257DBB4E6 Q35214400-BDED5740-C1C3-4AB4-9629-6FB3E005BB40 Q35590129-C0C6CE98-9144-4D54-A2B7-4E44E8BD500B Q36288790-EF643FAF-D6CC-47A0-B7E4-0BFBC0E6DF5B Q36802526-EACA1A4C-79F4-4E6F-B859-530EF5014484 Q37240517-F81D7BB2-B994-4259-8130-A9BAB59DA7F0 Q37240542-39B355E5-442E-4E47-9321-4F4A27BDBCB8 Q37240923-63B23AD1-B784-449A-96B2-EEC9C0D55019 Q37340904-7092777F-B529-4B6F-AFED-15B8EC818281 Q37612558-C3994A2A-11A4-4DA0-9345-07DF19F700AF Q38120510-68B249A2-B999-4035-A20F-9C5AD2A9D58A Q38221786-C46AE5D5-5EC9-4934-9A05-D51DBAC683D0 Q38273110-43CFB0CF-442A-4E70-855B-ED597D01B088 Q38299234-58ABD75F-3C8D-4676-A801-1363A7DB9DA5 Q38617959-FFDAD6B0-7572-495B-8DC4-963C42DFB6A8 Q38718282-CF872C30-1834-4E9E-88F2-F086E21164E0 Q38927110-F63136AF-9508-49CF-B6B2-6AF057322AD9 Q38951896-FBA2CE7D-EB13-4A0E-9B61-0D7D8F026B3A Q39123638-6C65FA89-6125-4564-BDFA-B8AFFA7F83FF Q39268666-0C029F39-B6AF-4490-B07C-DEB82FFEF582 Q39794749-A5E86C85-5CF2-44DF-A134-74199838C4FB Q39977051-FEBF89FD-C2A7-405E-9406-BC9725037102 Q40413149-38F933C9-82EE-405A-9FDF-841E939E95DF

P2860

Stepwise protein folding at near amino acid resolution by hydrogen exchange and mass spectrometry.

http://www.wikidata.org/entity/Q36835434

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

Stepwise protein folding at ne ...... xchange and mass spectrometry.

@en

type

label

Stepwise protein folding at ne ...... xchange and mass spectrometry.

@en

prefLabel

Stepwise protein folding at ne ...... xchange and mass spectrometry.

@en

P1433

Q36835434-2D1EE2D6-1AE6-41F3-B54D-A66D1DDFCD3F

P1476

Q36835434-7AD5F332-8A21-4E23-972C-5167812DACB4

P2093

Q36835434-05D724CE-74CF-439D-B5DA-0AF9C338701E

Q36835434-0BE1F864-BBF5-44CA-BC89-1705EB3CA45C

Q36835434-1EA403A8-DA96-4657-A121-589AB16E28BA

Q36835434-5548EEB4-22D4-4131-A05C-16BC2C14966A

Q36835434-8BCCE22F-6498-4C80-BF6E-E34C63F49CF8

Q36835434-A639B782-7344-46B5-B432-03288DC6A917

Q36835434-D57F57BB-9E9D-4ADD-82D6-C16A7587B6D7

P2860

Q36835434-01EDCAF1-06FF-46AE-975C-3D46AEB48CAD

Q36835434-08EDEA84-21EB-45EC-8DF3-B0D72D31F13C

Q36835434-0B375801-00E4-4BA2-8BC9-D52BAAEAA0AA

Q36835434-0CB3D5C2-92DA-4B55-B769-C9F57E31B02A

Q36835434-1B0F30C8-C302-4AB8-905C-B4018FEE1330

Q36835434-1B57E07B-37E1-4B21-A20C-7A6A27A53433

Q36835434-1C2313C2-384E-455C-9B6F-DD60C61CA38A

Q36835434-1E62F143-C4B5-4D11-8D5D-E01A6DADEEE4

Q36835434-20DB465D-4C7E-4450-90BB-0E8EDEC8AD0E

Q36835434-2DBC0A4C-8618-494D-A3AD-096975C22158

P304

Q36835434-2EB405E3-31D1-4A42-B195-30EC8A57FF37

P31

Q36835434-F2314D35-0840-4B61-ADE0-00AA9851B630

P356

Q36835434-AF8E3CCC-0351-4652-81D9-7EC4855D8F10

P407

Q36835434-B6DF0407-8E4E-4278-8C9D-9C208974E553

P433

Q36835434-6CCBDF82-203C-46F6-BD2C-EDC064C80C78

P478

Q36835434-337F3216-A3CB-462F-8B7E-AEBDA0528803

P577

Q36835434-E5E312F2-3B5D-49E9-8367-878174636167

P5875

Q36835434-5DE64EE9-BAE4-4EF4-8576-ED830F27B90A

P698

Q36835434-3B399283-2990-4BD4-A178-C19C0EE787CF

P921

Q36835434-D2EEDCBB-304A-41BD-A4B0-DE31D50FB91E

P932

Q36835434-A825F3D7-37A9-4282-99DC-34B99E9E64F1

P356

PNAS.1305887110

P1433

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

P1476

Stepwise protein folding at ne ...... xchange and mass spectrometry.

@en

P2093

Benjamin T Walters

http://www.w3.org/2001/XMLSchema#string

Laura E Rosen

http://www.w3.org/2001/XMLSchema#string

Leland Mayne

http://www.w3.org/2001/XMLSchema#string

S Walter Englander

http://www.w3.org/2001/XMLSchema#string

Susan Marqusee

http://www.w3.org/2001/XMLSchema#string

Wenbing Hu

http://www.w3.org/2001/XMLSchema#string

Zhong-Yuan Kan

http://www.w3.org/2001/XMLSchema#string

P2860

Levinthal's paradox

Taming the complexity of protein folding

Markov state model reveals folding and functional dynamics in ultra-long MD trajectories

Residual structure in unfolded proteins

Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study

From Levinthal to pathways to funnels

Nucleation mechanisms in protein folding

Discrete kinetic models from funneled energy landscape simulations

De novo prediction of protein folding pathways and structure using the principle of sequential stabilization

A simple model predicts experimental folding rates and a hub-like topology

P304

7684-7689

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.1305887110

http://www.w3.org/2001/XMLSchema#string

P407

P433

19

http://www.w3.org/2001/XMLSchema#string

P478

110

http://www.w3.org/2001/XMLSchema#string

P577

2013-04-19T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

236251944

http://www.w3.org/2001/XMLSchema#string

P698

23603271

http://www.w3.org/2001/XMLSchema#string

P921

protein folding

P932

3651421

http://www.w3.org/2001/XMLSchema#string