Similar Energetic Contributions of Packing in the Core of Membrane and Water-Soluble Proteins (Q27656426)

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Language	Label	Description	Also known as
English	Similar Energetic Contributions of Packing in the Core of Membrane and Water-Soluble Proteins	scientific article

Statements

instance of

scholarly article

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title

Similar Energetic Contributions of Packing in the Core of Membrane and Water-Soluble Proteins (English)

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main subject

catalysis

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author

Julian P Whitelegge

series ordinal

4

object named as

Julian P Whitelegge

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James U. Bowie

series ordinal

5

object named as

James U Bowie

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author name string

Nathan H Joh

series ordinal

1

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Amit Oberai

series ordinal

2

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Duan Yang

series ordinal

3

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language of work or name

English

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publication date

12 August 2009

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published in

Journal of the American Chemical Society

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volume

131

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issue

31

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page(s)

10846-7

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cites work

Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins

1 reference

stated in

PubMed Central

reference URL

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20 March 2017

Side-chain contributions to membrane protein structure and stability

1 reference

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PubMed Central

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20 March 2017

Structure of bacteriorhodopsin at 1.55 A resolution

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PubMed Central

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20 March 2017

Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect

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PubMed Central

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20 March 2017

Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding

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PubMed Central

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29 September 2017

Molecular packing and packing defects in helical membrane proteins

1 reference

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PubMed Central

reference URL

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29 September 2017

Polar residues drive association of polyleucine transmembrane helices

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PubMed Central

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29 September 2017

Helical membrane protein folding, stability, and evolution

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PubMed Central

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29 September 2017

Internal packing of helical membrane proteins

1 reference

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PubMed Central

reference URL

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29 September 2017

Structure-based prediction of the stability of transmembrane helix–helix interactions: The sequence dependence of glycophorin A dimerization

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PubMed Central

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29 September 2017

Crystallization of bacteriorhodopsin from bicelle formulations at room temperature

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PubMed Central

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27 November 2018

Computation and mutagenesis suggest a right-handed structure for the synaptobrevin transmembrane dimer

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27 November 2018

Helix-helix packing and interfacial pairwise interactions of residues in membrane proteins

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27 November 2018

Deciphering the message in protein sequences: tolerance to amino acid substitutions

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27 November 2018

Interhelical hydrogen bonding drives strong interactions in membrane proteins

1 reference

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PubMed

reference URL

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retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Side chains in transmembrane helices are shorter at helix-helix interfaces

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19603754

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A passive transmembrane helix

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19603754

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Perspectives: signal transduction. Proteins in motion

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19603754

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Asparagine-mediated self-association of a model transmembrane helix

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19603754

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1021/JA904711K

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Fatcat ID

release_bvaqr6d34bckflmmcnrwcrl4ba

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PMC publication ID

2744480

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PubMed publication ID

19603754

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ResearchGate publication ID

26672302

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