Mutational analysis of the N-capping box of the alpha-helix of chymotrypsin inhibitor 2.

scientific article

Mutational analysis of the N-capping box of the alpha-helix of chymotrypsin inhibitor 2. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1093/PROTEIN/7.6.777
P698PubMed publication ID7937708

P2093author name stringA R Fersht
N F elMasry
P433issue6
P921main subjectmutational analysisQ1955810
P304page(s)777-782
P577publication date1994-06-01
P1433published inProtein Engineering Design and SelectionQ15762396
P1476titleMutational analysis of the N-capping box of the alpha-helix of chymotrypsin inhibitor 2.
P478volume7

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cites work (P2860)
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Q24673351Helix capping
Q40425165Helix design, prediction and stability
Q30720275Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices
Q30377151Mapping side chain interactions at protein helix termini.
Q30325672Patterned library analysis: a method for the quantitative assessment of hypotheses concerning the determinants of protein structure.
Q44368454Role of an N(cap) residue in determining the stability and operator-binding affinity of Arc repressor.
Q41825033Sequence determinants of the capping box, a stabilizing motif at the N-termini of alpha-helices
Q28283891Sequence space, folding and protein design
Q72067207Stability and solvation of Thr/Ser to Ala and Gly mutations at the N-cap of alpha-helices
Q33883809The relationship between sequence and structure in elementary folding units
Q35886938The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding

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