Optimal local propensities for model proteins

scientific article published on 01 August 1995

Optimal local propensities for model proteins is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/PROT.340220411
P698PubMed publication ID7479714

P50authorRichard A. GoldsteinQ37380588
P2093author name stringGovindarajan S
P433issue4
P304page(s)413-418
P577publication date1995-08-01
P1433published inProteinsQ7251514
P1476titleOptimal local propensities for model proteins
P478volume22

Reverse relations

cites work (P2860)
Q74313144A metastable state in folding simulations of a protein model
Q31042817A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank
Q46877421Comparing folding codes for proteins and polymers
Q36280079Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold
Q34464266Contact order, transition state placement and the refolding rates of single domain proteins.
Q32160376Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein.
Q52251893Evolution of model proteins on a foldability landscape
Q42652304Favourable native-like helical local interactions can accelerate protein folding
Q52070055Identification and ab initio simulations of early folding units in proteins
Q47871365Intrahelical side chain interactions in alpha-helices: poor correlation between energetics and frequency
Q30176061Lattice models for proteins reveal multiple folding nuclei for nucleation-collapse mechanism 1 1Edited by A. R. Fersht
Q30428832Local interactions and the optimization of protein folding
Q41394376Local versus nonlocal interactions in protein folding and stability--an experimentalist's point of view
Q28303614Nucleation mechanisms in protein folding
Q33739669Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications
Q36472755Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet
Q36858393Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the alpha-helix fragment
Q77192762Statistical mechanics of protein folding by exhaustive enumeration
Q52950608Structural determinants of the rate of protein folding
Q34174860Tertiary DNA structure in the single-stranded hTERT promoter fragment unfolds and refolds by parallel pathways via cooperative or sequential events.
Q56999317The Highly Cooperative Folding of Small Naturally Occurring Proteins Is Likely the Result of Natural Selection
Q73665014The foldability landscape of model proteins
Q30176678The nucleation-collapse mechanism in protein folding: evidence for the non-uniqueness of the folding nucleus
Q37168015The ruggedness of protein-protein energy landscape and the cutoff for 1/r(n) potentials
Q38434620Use of conserved key amino acid positions to morph protein folds
Q52234198Use of quantitative structure-property relationships to predict the folding ability of model proteins
Q37651521Why are some proteins structures so common?

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