scholarly article | Q13442814 |
P50 | author | Andrew J Doig | Q42547635 |
P2093 | author name string | Rohl CA | |
P2860 | cites work | The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain | Q24519280 |
N- and C-capping preferences for all 20 amino acids in alpha-helical peptides | Q24675075 | ||
Three-dimensional structure of catalase from Penicillium vitale at 2.0 A resolution | Q27728944 | ||
Conformation of Polypeptides and Proteins | Q29617878 | ||
Hydrogen Bonded Helical Configurations of the Polypeptide Chain | Q33713566 | ||
Generalized Mathematical Relationships for Polypeptide Chain Helices: The Coordinates of the II Helix | Q33713793 | ||
Alpha-helix and mixed 3(10)/alpha-helix in cocrystallized conformers of Boc-Aib-Val-Aib-Aib-Val-Val-Val-Aib-Val-Aib-OMe | Q33833597 | ||
The polypeptide 310-helix | Q34017817 | ||
Helix geometry in proteins | Q34049849 | ||
Differences in the amino acid distributions of 3(10)-helices and alpha-helices | Q36277381 | ||
Incorporation of pairwise interactions into the Lifson-Roig model for helix prediction | Q36279249 | ||
Structural characteristics of alpha-helical peptide molecules containing Aib residues | Q37951600 | ||
Hydrogen bonding in globular proteins | Q40188265 | ||
Views of helical peptides: a proposal for the position of 3(10)-helix along the thermodynamic folding pathway | Q40493410 | ||
Addition of side chain interactions to modified Lifson-Roig helix-coil theory: application to energetics of phenylalanine-methionine interactions. | Q42003263 | ||
Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. | Q42244726 | ||
A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide | Q43022332 | ||
Effect of sequence-specific interactions on the stability of helical conformations in polypeptides | Q44136381 | ||
Molecular dynamics simulations of the unfolding of an alpha-helical analogue of ribonuclease A S-peptide in water | Q44354473 | ||
Determination of free energies of N-capping in alpha-helices by modification of the Lifson-Roig helix-coil therapy to include N- and C-capping. | Q44705720 | ||
Unfolding of an ?-helix in water | Q44974805 | ||
Short alanine-based peptides may form 3(10)-helices and not alpha-helices in aqueous solution | Q45971277 | ||
Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation | Q46099457 | ||
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide | Q46559748 | ||
Structure and function of cytochromes P450: a comparative analysis of three crystal structures. | Q49318994 | ||
Elucidating the folding problem of helical peptides using empirical parameters. | Q52376869 | ||
Alpha/3(10)-helix transitions in alpha-methylalanine homopeptides: conformational transition pathway and potential of mean force. | Q52385073 | ||
Thermodynamics and mechanism of alpha helix initiation in alanine and valine peptides. | Q52447787 | ||
Polypeptide Chain Configurations in Crystalline Proteins | Q55887295 | ||
The Structure of Fibrous Proteins | Q56038863 | ||
Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains | Q56522033 | ||
A Second Right-handed Helical Structure with the Parameters of the Pauling–Corey α-helix | Q59017414 | ||
Conformational preferences of oligopeptides rich in alpha-aminoisobutyric acid. II. A model for the 3(10)/alpha-helix transition with composition and sequence sensitivity | Q68181854 | ||
P433 | issue | 8 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 1687-1696 | |
P577 | publication date | 1996-08-01 | |
P1433 | published in | Protein Science | Q7251445 |
P1476 | title | Models for the 3(10)-helix/coil, pi-helix/coil, and alpha-helix/3(10)-helix/coil transitions in isolated peptides | |
P478 | volume | 5 |
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Q41896362 | Addition of side-chain interactions to 3(10)-helix/coil and alpha-helix/3(10)-helix/coil theory. |
Q42847580 | Determination of alpha-helix N1 energies after addition of N1, N2, and N3 preferences to helix/coil theory |
Q40539296 | Dissecting π-helices: sequence, structure and function |
Q36120585 | Early events in helix unfolding under external forces: a milestoning analysis |
Q34350870 | Effect of urea on peptide conformation in water: molecular dynamics and experimental characterization |
Q38270560 | Extension of a local backbone description using a structural alphabet: a new approach to the sequence-structure relationship. |
Q35963402 | Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin. |
Q28201207 | Occurrence, conformational features and amino acid propensities for the pi-helix |
Q58440528 | Peptide Secondary Structures as Molecular Switches |
Q33744698 | Phosphorylation of paxillin LD4 destabilizes helix formation and inhibits binding to focal adhesion kinase. |
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Q44033267 | Random-coil:α-helix equilibria as a reporter for the Lewis(X)-Lewis(X) interaction. |
Q35028531 | Recent advances in helix-coil theory. |
Q44290687 | Sequence and structure patterns in proteins from an analysis of the shortest helices: implications for helix nucleation |
Q37383095 | Stability and design of alpha-helical peptides. |
Q51858838 | Statistical mechanical model for helix-sheet-coil transitions in homopolypeptides. |
Q31049547 | Structure of a membrane-binding domain from a non-enveloped animal virus: insights into the mechanism of membrane permeability and cellular entry. |
Q53540139 | Temperature-dependent molecular dynamics study reveals an ionic liquid induced 310 - to α-helical switch in a neurotoxin. |
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Q34412832 | The influence of flanking secondary structures on amino Acid content and typical lengths of 3/10 helices |
Q24672547 | The pi-helix translates structure into function |
Q34199126 | The role of alpha-, 3(10)-, and pi-helix in helix-->coil transitions |
Q36438102 | Thermodynamics Of alpha-Helix Formation |
Q90443848 | Thermodynamics of helix formation in small peptides of varying length in vacuo, in implicit solvent, and in explicit solvent |
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