<p>The color scale on the right from black to blue indicates the density of the points for that region of the map.</p
α chain is shown in red and β chain in green. In the center of the groove, the peptide (chain C from...
The data files are labeled according to figure numbers in the associated Open Access article, H. R. ...
<p>The electron density map is contoured at 1.0σ level. The carboxyl product peptide ( violetpurple)...
<p>The residues (labeled) of the SH2 domain that form hydrogen bonds with at least one of the 12 pep...
<p>A. Cartoon representation of NRLLLTG-bound HSP70 SBD Molecule A. The SBD and NRLLLTG peptide are ...
<p>The red portion shows the hydrophilic side of the peptide and the green portion shows the hydroph...
<div><p>(A) Ribbon diagram showing peptide in yellow bound to side site of the β-appendage.</p> ...
Single-molecule measurements of complex biological structures such as proteins are an attractive rou...
<p>The H-bonds are highlighted in red. The different colors indicate the different locations of the ...
Secondary structure of proteins includes alpha helices (the most common), beta sheets, and other coi...
<p>Domains D2 and D3 are colored as in <a href="http://www.plosone.org/article/info:doi/10.1371/jour...
We used UV resonance Raman (UVRR) spectroscopy to quantitatively correlate the peptide bond AmIII3 f...
<p>585–1 & 18–1 peptide series are shown in in blue and red, respectively. Parent peptides are shown...
<p>The peptides (MLG in green, EEE in blue), the side chains of amino acids (in grey) interacting wi...
We used UV resonance Raman (UVRR) spectroscopy to quantitatively correlate the peptide bond AmIII3 f...
α chain is shown in red and β chain in green. In the center of the groove, the peptide (chain C from...
The data files are labeled according to figure numbers in the associated Open Access article, H. R. ...
<p>The electron density map is contoured at 1.0σ level. The carboxyl product peptide ( violetpurple)...
<p>The residues (labeled) of the SH2 domain that form hydrogen bonds with at least one of the 12 pep...
<p>A. Cartoon representation of NRLLLTG-bound HSP70 SBD Molecule A. The SBD and NRLLLTG peptide are ...
<p>The red portion shows the hydrophilic side of the peptide and the green portion shows the hydroph...
<div><p>(A) Ribbon diagram showing peptide in yellow bound to side site of the β-appendage.</p> ...
Single-molecule measurements of complex biological structures such as proteins are an attractive rou...
<p>The H-bonds are highlighted in red. The different colors indicate the different locations of the ...
Secondary structure of proteins includes alpha helices (the most common), beta sheets, and other coi...
<p>Domains D2 and D3 are colored as in <a href="http://www.plosone.org/article/info:doi/10.1371/jour...
We used UV resonance Raman (UVRR) spectroscopy to quantitatively correlate the peptide bond AmIII3 f...
<p>585–1 & 18–1 peptide series are shown in in blue and red, respectively. Parent peptides are shown...
<p>The peptides (MLG in green, EEE in blue), the side chains of amino acids (in grey) interacting wi...
We used UV resonance Raman (UVRR) spectroscopy to quantitatively correlate the peptide bond AmIII3 f...
α chain is shown in red and β chain in green. In the center of the groove, the peptide (chain C from...
The data files are labeled according to figure numbers in the associated Open Access article, H. R. ...
<p>The electron density map is contoured at 1.0σ level. The carboxyl product peptide ( violetpurple)...
DOI
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