Distribution of backbone conformation of hinge residues where (φ,ψ) is separated into four quadrants (please see Figure 4 for regions within each quadrant).

Fit of swapped and unswapped conformations of the hinge region to the electron density map.

Yamuna Kalyani Mathiharan (280666)
Anju Pappachan (280667)
H. S. Savithri (195807)
Mathur R. N. Murthy (148023)

February 2013

A) and B) show fit of swapped conformations to the electron density map (Fo-Fc; calculated after ...

Sparsely populated residue conformations in protein structures: Revisiting ``experimental'' Ramachandran maps

Kalmankar, Neha V
Ramakrishnan, C
Balaram, P

January 2014

The Ramachandran map clearly delineates the regions of accessible conformational (phi-) space for am...

Local Backbone Geometry Plays a Critical Role in Determining Conformational Preferences of Amino Acid Residues in Proteins

Balasco N.
Esposito L.
De Simone A.
Vitagliano L.

January 2022

The definition of the structural basis of the conformational preferences of the genetically encoded ...

Conformation of residues in hinge region for domain-swapped structure and non-domain swapped homologue.

Prashant Shingate (146643)
R. Sowdhamini (19238)

July 2012

A) Percent distribution of quadrant shifts of all hinge residues. B) Percent distribution of quad...

Backbone conformation of hinge regions in domain swapped oligomers.

Prashant Shingate (146643)
R. Sowdhamini (19238)

July 2012

A) (φ,ψ) conformation distribution of all hinge residues. B) (φ,ψ) conformation distribution of n...

Hinge residues tend to be on the surface, since steric clashes would often prevent them from being in the core

Samuel C Flores (42993)
Long J Lu (76480)
Julie Yang (76481)
Nicholas Carriero (7944)
Mark B Gerstein (32281)

December 2011

Copyright information:Taken from "Hinge Atlas: relating protein sequence to sites o...

Distribution of

Prashant Shingate (146643)
R. Sowdhamini (19238)

July 2012

values of non-hinge residues and hinge-residues from domain-swapped protomers and their respec...

Histogram of () (of glycine among NON-hinge residues, blue trace) and () (frequency of glycine among hinge residues, dashed red trace)

Samuel C Flores (42993)
Long J Lu (76480)
Julie Yang (76481)
Nicholas Carriero (7944)
Mark B Gerstein (32281)

December 2011

Copyright information:Taken from "Hinge Atlas: relating protein sequence to sites o...

The least conserved 20% of residues are significantly more likely to appear in hinges

Samuel C Flores (42993)
Long J Lu (76480)
Julie Yang (76481)
Nicholas Carriero (7944)
Mark B Gerstein (32281)

December 2011

Copyright information:Taken from "Hinge Atlas: relating protein sequence to sites o...

Backbone dihedral angle distributions of amino acids estimated from high-resolution crystal structures.

Martin Mechelke (582147)
Michael Habeck (93533)

June 2014

Density maps of distributions for Alanine (left column), Proline (middle column) and Glycine (ri...

Distribution of hydrogen bonds per residue in the given region of amino acid residues in four structural classes of proteins calculated with YASARA. Cases (A, C, E) without and (B, D, F) with energy minimization.

Anna V. Glyakina (338422)
Natalya S. Bogatyreva (239678)
Oxana V. Galzitskaya (198019)

February 2013

Distribution of hydrogen bonds per residue in the given region of amino acid residues in four str...

Statistics for swivel angles, bending angles and distributions of helix lengths.

Alexander Götz (488766)
Christina Scharnagl (1998736)

July 2018

(A) Classification by swivel angle (Φ) in bins with bin size of 45°. The highest populations for ...

Normalized amino acid propensities of the hinge residues with reference to amino acids at the loop regions.

Prashant Shingate (146643)
R. Sowdhamini (19238)

July 2012

Normalized amino acid propensities of the hinge residues with reference to amino acids at the loo...

Since active sites residues are enriched in hinges, we performed a separate conservation check on hinge residues in the 94 Hinge Atlas proteins with CSA annotation

Samuel C Flores (42993)
Long J Lu (76480)
Julie Yang (76481)
Nicholas Carriero (7944)
Mark B Gerstein (32281)

December 2011

Copyright information:Taken from "Hinge Atlas: relating protein sequence to sites o...

The distribution of RMSDs of nucleotide-residue conformations in relative to their center conformations of 800 classes.

Haotian Li (640676)
Yangyu Huang (472462)
Yi Xiao (135101)

March 2017

The distribution of RMSDs of nucleotide-residue conformations in relative to their center conform...

Fit of swapped and unswapped conformations of the hinge region to the electron density map.

Yamuna Kalyani Mathiharan (280666)
Anju Pappachan (280667)
H. S. Savithri (195807)
Mathur R. N. Murthy (148023)

February 2013

A) and B) show fit of swapped conformations to the electron density map (Fo-Fc; calculated after ...

Sparsely populated residue conformations in protein structures: Revisiting ``experimental'' Ramachandran maps

Kalmankar, Neha V
Ramakrishnan, C
Balaram, P

January 2014

The Ramachandran map clearly delineates the regions of accessible conformational (phi-) space for am...

Local Backbone Geometry Plays a Critical Role in Determining Conformational Preferences of Amino Acid Residues in Proteins

Balasco N.
Esposito L.
De Simone A.
Vitagliano L.

January 2022

The definition of the structural basis of the conformational preferences of the genetically encoded ...

Conformation of residues in hinge region for domain-swapped structure and non-domain swapped homologue.

Prashant Shingate (146643)
R. Sowdhamini (19238)

July 2012

A) Percent distribution of quadrant shifts of all hinge residues. B) Percent distribution of quad...

Backbone conformation of hinge regions in domain swapped oligomers.

Prashant Shingate (146643)
R. Sowdhamini (19238)

July 2012

A) (φ,ψ) conformation distribution of all hinge residues. B) (φ,ψ) conformation distribution of n...

Hinge residues tend to be on the surface, since steric clashes would often prevent them from being in the core

Samuel C Flores (42993)
Long J Lu (76480)
Julie Yang (76481)
Nicholas Carriero (7944)
Mark B Gerstein (32281)

December 2011

Copyright information:Taken from "Hinge Atlas: relating protein sequence to sites o...

Distribution of

Prashant Shingate (146643)
R. Sowdhamini (19238)

July 2012

values of non-hinge residues and hinge-residues from domain-swapped protomers and their respec...

Histogram of () (of glycine among NON-hinge residues, blue trace) and () (frequency of glycine among hinge residues, dashed red trace)

Samuel C Flores (42993)
Long J Lu (76480)
Julie Yang (76481)
Nicholas Carriero (7944)
Mark B Gerstein (32281)

December 2011

Copyright information:Taken from "Hinge Atlas: relating protein sequence to sites o...

The least conserved 20% of residues are significantly more likely to appear in hinges

Samuel C Flores (42993)
Long J Lu (76480)
Julie Yang (76481)
Nicholas Carriero (7944)
Mark B Gerstein (32281)

December 2011

Copyright information:Taken from "Hinge Atlas: relating protein sequence to sites o...

Backbone dihedral angle distributions of amino acids estimated from high-resolution crystal structures.

Martin Mechelke (582147)
Michael Habeck (93533)

June 2014

Density maps of distributions for Alanine (left column), Proline (middle column) and Glycine (ri...

Distribution of hydrogen bonds per residue in the given region of amino acid residues in four structural classes of proteins calculated with YASARA. Cases (A, C, E) without and (B, D, F) with energy minimization.

Anna V. Glyakina (338422)
Natalya S. Bogatyreva (239678)
Oxana V. Galzitskaya (198019)

February 2013

Distribution of hydrogen bonds per residue in the given region of amino acid residues in four str...

Statistics for swivel angles, bending angles and distributions of helix lengths.

Alexander Götz (488766)
Christina Scharnagl (1998736)

July 2018

(A) Classification by swivel angle (Φ) in bins with bin size of 45°. The highest populations for ...

Normalized amino acid propensities of the hinge residues with reference to amino acids at the loop regions.

Prashant Shingate (146643)
R. Sowdhamini (19238)

July 2012

Normalized amino acid propensities of the hinge residues with reference to amino acids at the loo...

Since active sites residues are enriched in hinges, we performed a separate conservation check on hinge residues in the 94 Hinge Atlas proteins with CSA annotation

Samuel C Flores (42993)
Long J Lu (76480)
Julie Yang (76481)
Nicholas Carriero (7944)
Mark B Gerstein (32281)

December 2011

Copyright information:Taken from "Hinge Atlas: relating protein sequence to sites o...

The distribution of RMSDs of nucleotide-residue conformations in relative to their center conformations of 800 classes.

Haotian Li (640676)
Yangyu Huang (472462)
Yi Xiao (135101)

March 2017

The distribution of RMSDs of nucleotide-residue conformations in relative to their center conform...

Fit of swapped and unswapped conformations of the hinge region to the electron density map.

Yamuna Kalyani Mathiharan (280666)
Anju Pappachan (280667)
H. S. Savithri (195807)
Mathur R. N. Murthy (148023)

February 2013

A) and B) show fit of swapped conformations to the electron density map (Fo-Fc; calculated after ...

Sparsely populated residue conformations in protein structures: Revisiting ``experimental'' Ramachandran maps

Kalmankar, Neha V
Ramakrishnan, C
Balaram, P

January 2014

The Ramachandran map clearly delineates the regions of accessible conformational (phi-) space for am...

Local Backbone Geometry Plays a Critical Role in Determining Conformational Preferences of Amino Acid Residues in Proteins

Balasco N.
Esposito L.
De Simone A.
Vitagliano L.

January 2022

The definition of the structural basis of the conformational preferences of the genetically encoded ...

Distribution of backbone conformation of hinge residues where (φ,ψ) is separated into four quadrants (please see <b>Figure 4</b> for regions within each quadrant).

Abstract

Extracted data

Distribution of backbone conformation of hinge residues where (φ,ψ) is separated into four quadrants (please see <b>Figure 4</b> for regions within each quadrant).

Abstract

Extracted data

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