[HTML][HTML] The interrelationships of side-chain and main-chain conformations in proteins
P Chakrabarti, D Pal - Progress in biophysics and molecular biology, 2001 - Elsevier
The accurate determination of a large number of protein structures by X-ray crystallography
makes it possible to conduct a reliable statistical analysis of the distribution of the main …
makes it possible to conduct a reliable statistical analysis of the distribution of the main …
Dependence of α-helical and β-sheet amino acid propensities on the overall protein fold type
K Fujiwara, H Toda, M Ikeguchi - BMC structural biology, 2012 - Springer
Background A large number of studies have been carried out to obtain amino acid
propensities for α-helices and β-sheets. The obtained propensities for α-helices are …
propensities for α-helices and β-sheets. The obtained propensities for α-helices are …
A conformational flexibility scale for amino acids in peptides
F Huang, WM Nau - Angewandte Chemie International Edition, 2003 - Wiley Online Library
The molecular flexibility of proteins is a crucial factor in determining their biological
activity,[1] including binding affinity,[2] antigenicity,[3] and enzymatic activity.[4] The …
activity,[1] including binding affinity,[2] antigenicity,[3] and enzymatic activity.[4] The …
Mitochondrial DNA depletion: mutations in thymidine kinase gene with myopathy and SMA
Background: The mitochondrial DNA (mtDNA) depletion syndrome (MDS) is an autosomal
recessive disorder of early childhood characterized by decreased mtDNA copy number in …
recessive disorder of early childhood characterized by decreased mtDNA copy number in …
Understanding the mechanism of β‐sheet folding from a chemical and biological perspective
M Jager, S Deechongkit, EK Koepf, H Nguyen… - Peptide …, 2008 - Wiley Online Library
Perturbing the structure of the Pin1 WW domain, a 34‐residue protein comprised of three β‐
strands and two intervening loops has provided significant insight into the structural and …
strands and two intervening loops has provided significant insight into the structural and …
Structure relaxation approximation (SRA) for elucidation of protein structures from ion mobility measurements (II). Protein complexes
Characterizing structures of protein complexes and their disease-related aberrations is
essential to understanding molecular mechanisms of many biological processes …
essential to understanding molecular mechanisms of many biological processes …
Synthesis and Structural Model of an α (2, 6)‐Sialyl‐T Glycosylated MUC1 Eicosapeptide under Physiological Conditions
S Dziadek, C Griesinger, H Kunz… - … –A European Journal, 2006 - Wiley Online Library
To study the effect of O‐glycosylation on the conformational propensities of a peptide
backbone, a 20‐residue peptide (GSTAPPAHGVTSAPDTRPAP) representing the full length …
backbone, a 20‐residue peptide (GSTAPPAHGVTSAPDTRPAP) representing the full length …
Engineered streptavidin monomer and dimer with improved stability and function
Although streptavidin's high affinity for biotin has made it a widely used and studied binding
protein and labeling tool, its tetrameric structure may interfere with some assays. A …
protein and labeling tool, its tetrameric structure may interfere with some assays. A …
Targeting the gatekeeper residue in phosphoinositide 3-kinases
A single residue in the ATP binding pocket of protein kinases—termed the gatekeeper—has
been shown to control sensitivity to a wide range of small molecule inhibitors (Chem. Biol …
been shown to control sensitivity to a wide range of small molecule inhibitors (Chem. Biol …
New insight into the solution structures of wheat gluten proteins from Raman optical activity
EW Blanch, DD Kasarda, L Hecht, K Nielsen… - Biochemistry, 2003 - ACS Publications
Vibrational Raman optical activity (ROA) spectra of the wheat proteins α-gliadin (A-gliadin),
ω-gliadin, and a 30 kDa peptide called TA-1 from the high molecular weight glutenin subunit …
ω-gliadin, and a 30 kDa peptide called TA-1 from the high molecular weight glutenin subunit …