RosettaCommons - Protein Design

Publication Type:

PubMed ID:

23563512

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=24313858

The designability of protein switches by chemical rescue of structure: mechanisms of inactivation and reactivation.

Sun, 22 Mar 2015 01:31:55 +0000

Authors:

Xia Y, DiPrimio N, Keppel TR, Vo B, Fraser K, Battaile KP, Egan C, Bystroff C, Lovell S, Weis DD, Anderson JC, Karanicolas J

Link to article:

Volume:

135

Year:

2013

Source:

J Am Chem Soc

Pages:

18840-9

Lab:

Karanicolas

Publication Subject:

Publication Type:

PubMed ID:

24313858

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=23159126

Design of a phosphorylatable PDZ domain with peptide-specific affinity changes.

Sun, 15 Mar 2015 19:10:44 +0000

Authors:

Smith CA, Shi CA, Chroust MK, Bliska TE, Kelly MJ, Jacobson MP, Kortemme T

Link to article:

Volume:

Year:

2013

Source:

Structure

Pages:

54-64

Lab:

Publication Subject:

Publication Type:

PubMed ID:

23159126

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=24244128

Computational protein design quantifies structural constraints on amino acid covariation.

Sun, 15 Mar 2015 19:10:18 +0000

Authors:

Ollikainen N, Kortemme T

Link to article:

Volume:

Year:

2013

Source:

PLoS Comput Biol

Pages:

e1003313

Lab:

Publication Subject:

Publication Type:

PubMed ID:

24244128

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=24255821

Amino-acid site variability among natural and designed proteins.

Sun, 15 Mar 2015 19:09:50 +0000

Authors:

Jackson EL, Ollikainen N, Covert AW 3rd, Kortemme T, Wilke CO

Link to article:

Volume:

Year:

2013

Source:

PeerJ

Pages:

e211

Lab:

Other Labs

Publication Subject:

Publication Type:

PubMed ID:

24255821

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=23139141

A comparison of successful and failed protein interface designs highlights the challenges of designing buried hydrogen bonds.

Sun, 15 Mar 2015 14:19:35 +0000

Authors:

Stranges PB, Kuhlman B

Link to article:

Volume:

Year:

2013

Source:

Protein Sci

Pages:

74-82

Lab:

Kuhlman

Publication Subject:

Publication Type:

NONE

PubMed ID:

23139141

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=21789164

Predicting the tolerated sequences for proteins and protein interfaces using RosettaBackrub flexible backbone design.

Sun, 15 Mar 2015 14:19:35 +0000

Authors:

Smith CA, Kortemme T

Link to article:

Volume:

Year:

2011

Source:

PLoS One

Pages:

e20451

Lab:

Publication Subject:

Publication Type:

PubMed ID:

21789164

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=23422426

Flexible backbone sampling methods to model and design protein alternative conformations.

Sun, 15 Mar 2015 14:19:35 +0000

Authors:

Ollikainen N, Smith CA, Fraser JS, Kortemme T

Link to article:

Volume:

523

Year:

2013

Source:

Methods Enzymol

Pages:

61-85

Lab:

Publication Subject:

Publication Type:

PubMed ID:

23422426

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=18547585

Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction.

Sun, 15 Mar 2015 13:45:01 +0000

Authors:

Smith CA, Kortemme T

Link to article:

Volume:

380

Year:

2008

Source:

J Mol Biol

Pages:

742-56

Lab:

Publication Subject:

Publication Type:

PubMed ID:

18547585

Status:

http://www.ncbi.nlm.nih.gov/pubmed/?term=18547586

A simple model of backbone flexibility improves modeling of side-chain conformational variability.

Sun, 15 Mar 2015 13:45:01 +0000

Authors:

Friedland GD, Linares AJ, Smith CA, Kortemme T

Link to article:

Volume:

380

Year:

2008

Source:

J Mol Biol

Pages:

757-74

Lab:

Publication Subject:

Publication Type:

PubMed ID:

18547586

Status: